ORIGINAL ARTICLE | BREAST CANCER
10 (e010); 1-37
DOI: 10.21106/IJTMRPH_266_2026

Network Pharmacology and Preliminary In-Vitro Evaluation of Piper Longum (Indian Long Pepper) in Breast Cancer

Department of Biotechnology, All India Institute of Medical Sciences, New Delhi, India;
Department of Radiation Oncology, Dr. B. R. Ambedkar Institute Rotary Cancer Hospital, All India Institute of Medical Sciences, New Delhi, India;
Department of Biochemistry, All India Institute of Medical Sciences, New Delhi, India;
Department of Roga Nidan and Vikriti Vigyan (Pathology), All India Institute of Ayurveda (AIIA), New Delhi, India;
Department of Kaya Chikitsa (Internal Medicine), All India Institute of Ayurveda (AIIA), Goa, India.
Author image

*Joint corresponding authors.

*Corresponding authors: Shivam Singh, Vitthal Govindappa Huddar, Subhash Gupta shivam10singh2020@gmail.com drvghuddar@gmail.com drsubhashgupta72@gmail.com All India Institute of Medical Sciences, New Delhi, India

Licence
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ABSTRACT

Background and Objectives

Piper longum (Indian Long Pepper) contains phytochemicals reported to have anticancer activity, but their targets and effects in breast-cancer models remain uncertain. This exploratory study combined network pharmacology, analysis of public breast cancer data, molecular docking, MCF-7 viability, DNA cell cycle, and apoptosis assays.

Methods

Nineteen compounds from P. longum fruit were identified using the literature and phytochemical databases. Target prediction tools and cancer gene databases were used to identify interactions with breast cancer genes. Protein–protein interaction, gene ontology, and pathway analyses highlighted key targets. Molecular docking was used to evaluate binding affinities, and in vitro assays assessed cytotoxicity in MCF-7 breast cancer cells.

Results

This study revealed 600 common gene targets between P. longum compounds and breast cancer. Compound-target-disease network analysis prioritized Norcepharadione B, Aristolodione, Pellitorine, Aristolactam AII, and N-isobutyl decadienamide as candidate compounds. Significant breast cancer genes (TP53, CTNNB1, STAT3, SMAD3, EGFR, and HSP90AA1) were central to these interactions. Notably, HSP90AA1 showed the most favorable predicted docking scores with Norcepharadione B and Aristolactam AII. Additionally, the aqueous extract of P. longum significantly inhibited the MCF-7 MTT signal, with an IC50 of 3.75 µg/mL.

Conclusion and Implications for Translation

In this study, Piper longum phytochemicals were linked to key cancer genes. Molecular docking of the top five compounds with six genes showed that Norcepharadione B had the strongest affinity for HSP90AA1, indicating its potential to modulate HSP90AA1-mediated pathways, including ER and HER2 signaling. These interactions suggest therapeutic relevance. Furthermore, aqueous P. longum extract inhibited MCF-7 cellular metabolism at the IC₅₀ dose, possibly through cell-cycle arrest or apoptosis, which is currently under further investigation in our laboratory. These findings support further testing of defined P. longum compounds in breast-cancer models, but they do not yet establish therapeutic activity or mechanism.

Keywords

Breast Cancer
Piper Longum
Network Pharmacology
Molecular Docking
Cell Proliferation

INTRODUCTION

Background

Breast cancer continues to be a significant challenge in global health, as its complex development and varied clinical presentations pose substantial difficulties for effective treatment and prevention.[1] With the worldwide occurrence of this disease on the rise, it is crucial to explore the intricate nature of breast cancer to create successful therapeutic approaches.[2]

Network pharmacology is widely used to prioritize compound-target relationships in complex mixtures, although its predictions require experimental validation. Unlike conventional single-target approaches, it enables the identification of multi-target mechanisms underlying the therapeutic effects of complex herbal medicines. In the present study, network pharmacology was employed to predict the potential molecular targets and biological pathways through which Piper longum phytochemicals may exert anti-breast cancer activity.

Piper longum (Indian long pepper) is a medicinal plant of the family Piperaceae that has long been used in traditional medicine and has attracted increasing attention for its anticancer potential.[3] Experimental studies have shown that P. longum extracts and several of its bioactive constituents, including piperine and piperlongumine, inhibit breast cancer cell proliferation through mechanisms involving apoptosis, cell-cycle arrest, oxidative stress, and modulation of multiple oncogenic signaling pathways.[4,5] However, the comprehensive molecular targets and interconnected signaling networks through which the diverse phytochemicals of P. longum exert their anti-breast cancer effects remain poorly understood. Therefore, this study used an integrated network pharmacology, molecular docking, and experimental approach to systematically identify the anti-breast cancer activity of P. longum.

Objectives

This study used network analysis to prioritize P. longum phytochemicals and breast-cancer-associated targets for further testing. The process involved several key steps, including gathering and organizing data on the chemical compounds present in P. longum, constructing a network using analytical methods, identifying key nodes through network analysis, computationally predicting results using molecular docking, and interpreting the findings to predict potential drug targets and therapeutic uses. In addition, the effect of P. longum aqueous extract on cancer cell proliferation was also assessed in the MCF-7 breast cancer cell line.

Aim

The study aimed to investigate different compounds found in P. longum as potential phytochemicals against breast cancer and to explore the effect of the aqueous extract of P. longum fruits on breast cancer cell proliferation.

METHODS

P. longum Bioactive Compounds Identification

Bioactive phytochemical constituents reported from the fruits of Piper longum were compiled using two independent sources: (i) the Indian Medicinal Plants, Phytochemistry and Therapeutics (IMPPAT) database (https://cb.imsc.res.in/imppat/; accessed on 25 April 2025), and (ii) a systematic literature survey of published phytochemical studies.[6] The IMPPAT database was searched using the keyword “Piper longum” under the medicinal plant search option. All phytochemicals specifically annotated for the fruit of P. longum were retrieved. Literature searches were performed using combinations of the keywords “Piper longum,” “fruit,” “phytochemical,” “constituents,” “secondary metabolites,” and “chemical composition.”

The lists obtained from both sources were merged, and duplicate compounds were removed using compound names and PubChem Compound Identifiers (CID). Only compounds with a defined chemical structure and an available PubChem entry were retained for further analysis. Canonical SMILES and molecular structures were downloaded from PubChem and used as input for subsequent analyses (https://pubchem.ncbi.nlm.nih.gov/).[7] All databases were accessed during 2024.

Screening of Potential Bioactive Compounds Using Absorption, Distribution, Metabolism, and Excretion (ADME) Analysis

The collected phytochemical compounds were subjected to pharmacokinetic evaluation using the SwissADME web server (http://www.swissadme.ch/) to assess their drug-likeness and suitability for oral administration.[8] The canonical SMILES notation for each compound, obtained from the PubChem database, was uploaded to the SwissADME server for analysis. Several physicochemical and pharmacokinetic parameters relevant to drug discovery were evaluated, including molecular weight, hydrogen bond donor and acceptor counts, topological polar surface area (TPSA), XLOGP3 (octanol/water partition coefficient), predicted gastrointestinal (GI) absorption, Lipinski’s Rule of Five compliance, and the predicted bioavailability score.[4,9] These parameters were selected to assess the oral drug-likeness, pharmacokinetic behavior, and medicinal chemistry suitability of each phytochemical.

Compounds were screened using predefined inclusion criteria to select candidates with favorable pharmacokinetic properties. Only compounds with complete physicochemical information in SwissADME, a canonical chemical structure available in the PubChem database, no violations of Lipinski’s Rule of Five, a predicted bioavailability score ≥ 0.30, and acceptable GI absorption were considered eligible for further analysis. The Lipinski rule is based on specific physicochemical properties, such as absorption, distribution, metabolism, and excretion, to predict drug pharmacokinetic properties such as (1) a maximum of five hydrogen bond donors, (2) a maximum of 10 hydrogen bond acceptors, (3) a molecular mass less than 500 Da, and (4) the partition coefficient, or XLOGP3, must not exceed 5 (Supplementary Table 2). The partition coefficient quantifies the relationship between a compound’s lipophilicity (fat solubility) and hydrophilicity (water solubility). A compound with XLOGP3 > 5 is considered excessively lipophilic. Such compounds often suffer from several pharmacokinetic problems, including poor aqueous solubility in fluids such as GI fluids, reduced intestinal absorption, excessive tissue accumulation, and more. Conversely, compounds were excluded if they lacked complete structural or physicochemical information, were unavailable in the PubChem database, violated one or more of Lipinski’s criteria, exhibited poor predicted GI absorption, or had a predicted bioavailability score below 0.30 because in early drug discovery, compounds with a bioavailability score of ≥0.3 are generally considered acceptable, whereas values >0.5 are preferred for improved therapeutic efficacy and dose optimization.[10] After applying these screening criteria, 19 phytochemical compounds were identified as potential bioactive constituents of Piper longum and were subsequently selected for downstream target prediction and network pharmacology analyses. Supplementary Figure 1 shows a brief flow diagram of the screening pipeline.

P. longum Potential Targets Prediction

The potential human protein targets of the 19 phytochemicals that passed the predefined ADME and drug-likeness criteria were predicted using three complementary in silico platforms: SuperPred (https://prediction.charite.de/; accessed on 10th May 2025), SwissTargetPrediction (http://www.swisstargetprediction.ch/; accessed on 10th May 2025), and DIGEP-Pred (http://www.way2drug.com/ge/; accessed on 10th May 2025).[11–13] Canonical SMILES structures obtained from PubChem were used as input for target prediction. Targets meeting the predefined confidence criteria were retained for subsequent analysis. Specifically, predicted targets with a probability score >0.80 in SuperPred, >0.40 in SwissTargetPrediction, and >0.50 in DIGEP-Pred were selected.[14] The search was restricted to Homo sapiens targets. Predicted target names, UniProt identifiers, gene symbols, and probability scores were retrieved. Duplicate targets predicted for multiple compounds were merged before downstream analyses. The resulting target lists from the three platforms were integrated to generate a comprehensive set of candidate targets associated with the selected P. longum phytochemicals. These targets represent computational predictions and database-derived associations and were not considered experimentally validated molecular targets.

Breast Cancer Screening Targets

Breast cancer-associated genes were retrieved from the Online Mendelian Inheritance in Man (OMIM) (https://www.omim.org/; accessed on 12th May 2025), Therapeutic Target Database (TTD) (https://db.idrblab.net/ttd/; accessed on 12th May 2025), and GeneCards (https://www.genecards.org/; accessed on 13th May 2025) (with a relevance score exceeding 30) using the keyword “Breast Cancer.”[15–17] The predefined database-specific criteria for human protein-coding genes were applied. Database-specific inclusion criteria were applied, gene symbols were standardized, and duplicate entries were removed. The resulting disease-associated gene set was then compared with the predicted phytochemical target set to identify shared candidate targets.

Shared Target Identification

The predicted P. longum phytochemical targets and breast cancer-associated genes were compared using Venny version 2.1.0 (https://bioinfogp.cnb.csic.es/tools/venny/; on 15th May 2025). The overlapping genes were considered shared candidate targets linking the selected phytochemicals with breast cancer. They were subsequently subjected to PPI-network construction, enrichment analysis, compound–target–disease network analysis, and molecular docking.

Construction and Analysis of Protein–Protein Interaction (PPI) Network

Protein-protein interactions (PPIs) play a crucial role in regulating cellular activities and biological functions across different organisms. Gaining insights into protein interactions can enhance our understanding of infection mechanisms and inform the development of effective drugs and treatment strategies. A PPI network was constructed using the STRING database (https://string-db.org/; 16th May 2025), focusing on Homo sapiens genes with high-confidence interaction scores of ≥0.7, with disconnected nodes hidden.[18] Next, network data from the STRING database were exported as a tab-separated values file to build the PPI network diagram and perform enrichment analysis using Cytoscape v3.9.1.[19] Network topology was analyzed using the CytoNCA plugin by calculating Degree Centrality (DC), Betweenness Centrality (BC), and Closeness Centrality (CC) for each node. Degree centrality was used to identify highly connected proteins, while betweenness and closeness centrality were used to evaluate each node’s relative influence and connectivity within the network.

Construction and Analysis of Compound, Target, and Disease (C-T-D) Network

A C-T-D network was developed using Cytoscape v3.9.1 (https://cytoscape.org/) to visualize interactions among the selected phytochemicals, predicted target genes, and breast cancer. We extracted nodes representing core genes, drugs, and diseases. By analyzing the nodes, we identified several targets based on their connectivity degree, which reflects their importance. We used the CytoNCA plugin to perform network topology analysis and loaded the C-T-D network map into Cytoscape version 3.9.1. Nodes were ranked by degree centrality. Degree was used as a network prioritization measure, not to test statistical significance.[20] Nodes with higher degree values were considered more influential within the network, and the top-ranked phytochemicals were identified based on their connectivity to predicted target genes.

Gene Ontology (GO) Analysis for Enrichment and Pathway Analysis

ShinyGO 0.7 (http://bioinformatics.sdstate.edu/go/; accessed on 20th May 2025) was utilized for the analysis of pathway and process enrichment.[21] This tool encompasses a standard collection of ontologies for enrichment analysis, including Gene Ontology (GO) processes, Kyoto Encyclopedia of Genes and Genomes (KEGG) pathways, Reactome gene sets, canonical pathways, and a thorough resource for mammalian protein complexes. GO and KEGG enrichment analyses were performed on the 23 top-ranked genes selected from the PPI network.[22]

Analysis of Gene Expression

Gene expression analysis was performed using the Gene Expression Profiling Interactive Analysis 2 (GEPIA2, http://gepia.cancer-pku.cn/; accessed on 22nd May 2025), which integrates RNA-sequencing data from The Cancer Genome Atlas (TCGA) and the Genotype-Tissue Expression (GTEx) projects.[23] Breast Invasive Carcinoma (BRCA) tumor samples were compared with normal breast tissues using the GEPIA2 “Expression DIY” module. The differential expression cut-off parameters were set to |log2FC| ≥ 1 and p < 0.01, consistent with previous reports.[24] At the time of analysis, the BRCA dataset comprised 1,085 tumor samples and 291 normal samples (TCGA and GTEx combined). Differential expression analysis was performed using the statistical methods implemented in the GEPIA2 platform. GEPIA2 uses ANOVA for differential expression between tumor and normal tissues and the log-rank test for survival analysis.

Analysis of Overall Survival and Heat Map of Survival

Overall survival analysis of the six hub genes was performed using the GEPIA2 survival module with the default parameters.[25] Patients were automatically divided into high- and low-expression groups according to the default GEPIA2 expression cut-off (median expression), and survival differences were evaluated using Kaplan–Meier survival curves and the log-rank test. The GEPIA2 server generated hazard ratios with 95% confidence intervals. Because survival analysis was performed only for six predefined hub genes identified through the network analysis, no additional multiple-testing correction was applied.

Molecular Docking

The PDB structural data of the six hub genes were obtained from the Protein Data Bank (PDB) (https://www.rcsb.org/; accessed on 25th May 2025).[26] The PyMOL Molecular Graphics System, Version 2.3.2, developed by Schrödinger, LLC (http://www.pymol.org/pymol), was then used to view the downloaded target structure files in .pdb format.[27] Using PyMOL, water molecules and other heteroatoms, such as Ca, Cl, and Na, were removed from the structures before energy minimization. Then, using PubChem (https://pubchem.ncbi.nlm.nih.gov/), the top five bioactive compounds (ligands) from P. longum were converted into their corresponding 3D conformations in the .sdf file format.[2] Subsequently, the target molecules in .pdb format and ligand molecules in .sdf format were loaded into the cavity-detection guided blind docking program CB-Dock2 (http://cadd.labshare.cn/cb-dock2/; accessed on 25th May 2025).[28] CB-Dock2 automatically identifies potential ligand-binding cavities within the protein structure and ranks the predicted cavities according to their size. Based on the predicted cavities, the docking center and docking box dimensions are automatically determined according to the ligand structure. Molecular docking is subsequently performed using AutoDock Vina (https://github.com/ccsb-scripps/AutoDock-Vina). The resulting ligand-binding poses are ranked according to their predicted Vina scores, expressed in kcal/mol. These values represent the predicted binding affinity/docking scores of the corresponding protein–ligand complexes, with more negative values indicating a more favorable predicted interaction.

The top-ranked conformation for each protein–ligand complex was considered the optimal predicted binding pose. Finally, 2D schematic representations of predicted protein-ligand interactions were further visualized using two-dimensional interaction diagrams generated with the LIGPLOT tool (https://www.ebi.ac.uk/thornton-srv/software/LigPlus/; accessed on 25th May 2025) with standard Protein Data Bank file input.[29] The result is a PostScript file, in color or black and white, that identifies hydrogen bonds, hydrogen-bond distances, interacting amino acid residues, and hydrophobic contacts between the ligands and the respective target proteins.

Extract Preparation

Dried fruits of Piper longum Linn. were procured from the pharmacy of the All India Institute of Ayurveda (AIIA), New Delhi, India. The plant material was authenticated in the Department of Dravyaguna, AIIA, before use in accordance with institutional quality-control procedures and the standards of the Ayurvedic Pharmacopoeia of India. The fruits were thoroughly washed with distilled water to remove adhering dust, foreign particles, and damaged plant material, then shade-dried at ambient temperature for approximately 20 days until a constant weight was achieved. The dried fruits were then pulverized into a coarse powder using an electric grinder and stored in airtight containers under dry conditions until extraction.

To compare different extraction approaches, aqueous and hydroalcoholic extracts were prepared using both cold maceration and Soxhlet extraction techniques at the Department of Rog Nidan and Vikriti Vigyan, AIIA. For cold maceration, 400 g of the powdered fruit material was suspended in 5 L of sterile double-distilled water (solid-to-solvent ratio, 1:12.5 w/v) and continuously stirred at room temperature (25 ± 2°C) for 12 hours to facilitate efficient extraction of water-soluble phytoconstituents. The extract was subsequently filtered through Whatman No. 1 filter paper to remove insoluble plant debris.

For Soxhlet extraction, coarsely powdered P. longum fruits were extracted separately with distilled water and a hydroalcoholic solvent (water, 1:1, v/v) until the extraction solvent in the siphon tube became colorless, indicating exhaustive extraction of soluble constituents. The resulting extracts were filtered through Whatman No. 1 filter paper to remove particulate matter.

The filtrates from all extraction methods were concentrated by evaporation in a hot-air oven at 55°C for 24 hours until a semisolid crude extract was obtained. The dried extracts were transferred to sterile airtight containers and stored at 4°C until further use. The extraction yield percentage was calculated as follows:

Extraction yields (%)=Weight  of  driedextract(g)Weight  of  driedplant  material(g)×100

The extraction yields are given in (Supplementary Table 1).

HIGH PERFORMANCE THIN LAYER CHROMATOGRAPHY (HPTLC)

Piperine is one of the most abundant and essential alkaloids found in the Piperaceae family, such as P. longum and P. nigrum. Therefore, the selected extracts were chemically standardized by HPTLC using piperine as the reference marker before biological evaluation. A simple, rapid, quantitative HPTLC technique was used to validate the presence of piperine in various P. longum extracts mentioned above, following the HPTLC Association protocol for P. longum (www.hptlc-association.org). Briefly, 1 mg of test samples (cold maceration aqueous extract, aqueous, and hydro-alcoholic extracts by the Soxhlet method) was dissolved in 1 mL of methanol. Similarly, 1 g of dried fruit powder was dissolved in 10 mL of methanol, and 0.9 mg of standard piperine (Sigma-Aldrich, USA) was dissolved in 1 mL of methanol. Each standard and extract solution was sonicated for 10 minutes. The plate was prepared according to the HPTLC software. A mobile phase comprising Cyclohexane: Ethyl acetate (5:3 v/v) was prepared, and 20 mL of it was added to the chromatographic glass chamber. Two saturation pads were placed in the chamber for 20 minutes. Meanwhile, 7 µL of test samples and 3 µL of serially diluted piperine standard solutions were applied to pre-coated HPTLC Si 60 F254 (Merck) plates. After loading and saturation, the silica gel plate was placed in the mobile phase to allow the samples to develop in the solvent. Following absorption, the plate was air-dried. The underivatized plate was viewed under UV light at 254 nm and 366 nm to compare piperine bands in test samples with standards. Piperine detection was also performed after derivatization.

Cell Culture

The human breast adenocarcinoma cell line MCF-7, obtained from the National Center for Cell Science (NCCS), Pune, India, was maintained in Dulbecco’s Modified Eagle Medium (DMEM) supplemented with 10% heat-inactivated fetal bovine serum (FBS), 100 U/mL penicillin, and 100 μg/mL streptomycin. Cells were cultured in a humidified incubator at 37°C with 5% CO₂ and 95% air. The culture medium was replaced every 2–3 days, and cells were passaged at approximately 70–80% confluency using 0.25% trypsin–EDTA. Cell viability was routinely assessed by the trypan blue exclusion assay, and only cultures with>95% viability and no visible contamination were used for experiments. For treatment studies, cells were seeded at the required density and allowed to adhere for 24 hours before exposure to the test extracts.

Preparation of Extract Dilutions

A stock solution of the aqueous P. longum extract was prepared at 1 mg/mL in phosphate-buffered saline (pH 7.4) and filter-sterilized before use. Immediately before each experiment, serial working dilutions were freshly prepared from the stock solution using complete culture medium to obtain final treatment concentrations of 0.25, 0.5, 1.0, 2.5, 3.75, 5.0, 7.5, 10, 12.5, 15, 20, 25, 30, and 50 µg/mL. Cells treated with complete culture medium alone served as the untreated control.

MTT Assay

The cytotoxic effect of Piper longum aqueous extract on MCF-7 human breast cancer cells was evaluated using the 3-(4,5-dimethylthiazol-2-yl)-2,5-diphenyltetrazolium bromide (MTT) assay. Briefly, 1 × 104 MCF-7 cells were seeded into 96-well flat-bottom tissue culture plates at an appropriate density and allowed to attach overnight under standard culture conditions. The next day, the culture medium was replaced with fresh complete medium containing different concentrations of P. longum aqueous extract. Untreated cells maintained in complete culture medium served as the negative control.

After 24 hours of treatment, 20 μL of MTT solution (5 mg/mL prepared in phosphate-buffered saline) was added to each well, followed by incubation for an additional 4 hours at 37°C in a humidified atmosphere containing 5% CO₂. During this period, metabolically active cells reduced the yellow tetrazolium salt to insoluble purple formazan crystals. At the end of the incubation period, the culture medium containing excess MTT reagent was carefully aspirated without disturbing the crystals, and 100 μL of dimethyl sulfoxide (DMSO) was added to each well to completely dissolve the formazan crystals. The plates were gently agitated for 10–15 minutes to ensure complete solubilization before measuring the absorbance at 570 nm using a microplate reader. Cell viability was expressed as the percentage of viable cells relative to the untreated control using the following equation:

Cell viability(%)=Absorbance  of  treated  cellsAbsorbance  of  control  cells×100

The concentration of P. longum aqueous extract required to inhibit 50% of cell viability (IC₅₀) was determined from the dose-response curve in GraphPad Prism version 10. Each concentration was tested in [number] technical wells in each of [number] independent experiments. Data are presented as mean ± SD.

Statistical Analysis

All experiments were performed in three independent biological replicates, with each treatment and control analyzed in triplicate wells. Data are expressed as the mean ± standard deviation (SD). Statistical analyses were performed using GraphPad Prism version 10.0 (GraphPad Software, San Diego, CA, USA). The half-maximal inhibitory concentration (IC₅₀) of P. longum aqueous extract was determined by nonlinear regression analysis using a log(inhibitor) vs. normalized response (variable slope) dose-response curve model. A p-value of <0.05 was considered statistically significant.

RESULTS

P. longum Active Compounds

Literature review and IMPPAT database searches identified 82 bioactive compounds in P. longum fruit (Supplementary Table 2). All compounds were evaluated using SwissADME analysis to assess drug-likeness based on bioavailability score ≥0.3 and Lipinski’s rule of five, which is used to predict the drug pharmacokinetic properties based on the facts such as (1) a maximum of five hydrogen bond donors, (2) a maximum of 10 hydrogen bond acceptors, (3) a molecular mass less than 500 Da, and (4) the partition coefficient, or XLOGP3, must not exceed 5 (Supplementary Table 3). This screening yielded 19 promising ligands (Supplementary Table 2). The selected compounds had calculated molecular weights of approximately 222-370 Da and XLOGP3 values of 1.23–4.70. Predicted GI absorption and blood-brain barrier penetration have also been reported separately for each compound in Supplementary Table 3. Additionally, most compounds were not P-glycoprotein (PGP) substrates, suggesting reduced efflux and enhanced bioavailability and reinforcing their potential as effective therapeutic candidates.

Breast Cancer and P. longum Potential Targets

Following the ADME analysis, the bioactive compounds underwent target prediction using the SuperPred, SwissTargetPrediction, and DIGEP-Pred databases, yielding 11,812 predicted targets. A thorough search using the keyword “Breast Cancer” in OMIM, the TTD, and GeneCards identified 954 target genes. After reviewing the target genes linked to P. longum and breast cancer, we found an overlap of 600 targets, as shown in Figure 1b and listed in Supplementary Table 4.

(a) Predicted BOILED-Egg diagram of the selected compounds. BBB - Blood Brain Barrier, HIA - Human Intestinal Absorption, PGP+ - substrate of P-glycoprotein and PGP- - non-substrate of P-glycoprotein. (b) Intersecting targets between the active phytochemical potential protein targets in <em>P. longum</em> and Breast cancer-related genes. (c) The PPI network of the 600 intersecting targets, (d) The PPI network of the top 23 target genes, and (e) Compound – Target – Disease network of breast cancer and <em>P. longum.</em>
Figure 1.
(a) Predicted BOILED-Egg diagram of the selected compounds. BBB - Blood Brain Barrier, HIA - Human Intestinal Absorption, PGP+ - substrate of P-glycoprotein and PGP- - non-substrate of P-glycoprotein. (b) Intersecting targets between the active phytochemical potential protein targets in P. longum and Breast cancer-related genes. (c) The PPI network of the 600 intersecting targets, (d) The PPI network of the top 23 target genes, and (e) Compound – Target – Disease network of breast cancer and P. longum.

Protein–Protein Interaction (PPI) Network

Of the 600 overlapping targets, 516 were included in the STRING interaction network under the predefined high-confidence interaction threshold, whereas the remaining targets were excluded because they lacked qualifying interactions. To refine the analysis, we ranked nodes by degree and generated a focused PPI network of the top 23 genes using Cytoscape (Figure 1d). These genes included TP53, CTNNB1, STAT3, EP300, BRCA1, JUN, HDAC1, SMAD3, FOXO3, EGFR, HIF1A, CREBBP, HSP90AA1, CDK2, SMAD2, CDK4, SMARCA4, ATM, GRB2, CDKN1B, PTPN11, CD44, and SHC1.

The refined network consisted of 23 nodes and 139 edges, with an average of 12.1 neighbors per node. Degree centrality (DC), betweenness centrality (BC), and closeness centrality (CC) values are provided in Supplementary Table 5. DC quantifies the total number of direct connections a node possesses. DC reflects the number of direct connections, BC indicates a node’s role in shortest paths, and CC measures proximity to all nodes.[30] Six genes—TP53, CTNNB1, STAT3, SMAD3, EGFR, and HSP90AA1—showed above-average DC, BC, and CC, identifying them as hub genes (Supplementary Table 5). The network hierarchy for hub gene selection is as follows:

600 overlapping targets → 516 STRING-network nodes → Cytoscape → CytoNCA → Degree, Betweenness Centrality (BC), and Closeness Centrality (CC) → 23 top-ranked network genes → 6 final hub genes.

Construction and Analysis of C-T-D Network

The Cytoscape application was used to create a compound-target-disease network, enabling exploration of the complex interactions among compounds, targets, and breast cancer. Figure 1e depicts the C-T-D network, which encompasses 200 nodes and 400 edges, with an average of 4 neighboring nodes. Supplementary Table 6 presents the degree, betweenness, and closeness centralities for the top 15 bioactive compounds associated with breast cancer. The five compounds with the highest degree centrality were Pellitorine (20), Aristolodione (18), Aristolactam AII (18), Norcepharadione B (16), and N-isobutyl decadienamide (15).

Gene Ontology (GO) Enrichment and KEGG Pathway Analysis

Targets of P. longum were analyzed using functional annotation and enrichment analyses, revealing key biological roles associated with its phytochemicals. Gene Ontology (GO) and KEGG enrichment analyses were performed on the 23 top-ranked genes selected from the PPI network. Gene Ontology (GO) analysis showed involvement in biological processes (BP) such as responses to growth factors, regulation of signal transduction, and responses to chemical and oxygen-containing stimuli. Cellular components (CC) included SMAD complexes, cyclin-dependent kinase complexes, transcription repressor complexes, euchromatin, DNA repair complexes, and chromosomes. Molecular functions (MF) comprised p53 binding, transcription coactivator binding, kinase and phosphatase binding, and transcription regulation. Using an FDR cutoff of 0.05, 631 BP, 19 CC, and 74 MF terms were identified across 23 genes (Supplementary Figure 2). KEGG pathway analysis revealed 101 associated pathways, including cancer-related pathways, breast cancer, chronic myeloid leukemia, microRNAs in cancer, Forkhead box O (FOXO) signaling, PI3K-Akt signaling, cell cycle regulation, viral carcinogenesis, and hepatitis C. These findings highlight the therapeutic relevance of P. longum.

Unique Gene Expression

We assessed the expression levels of six breast cancer hub genes, including TP53, CTNNB1, STAT3, SMAD3, EGFR, and HSP90AA1, by comparing them with the BRCA dataset using the GEPIA2 web tool (Supplementary Figure 3). The Cancer Genome Atlas-BRCA (TCGA_BRCA) dataset comprises expression data from 1,085 tumor tissues and 291 corresponding normal tissues related to BRCA. In the box plot, tumor samples are represented in red, while normal samples are shown in grey. A red asterisk indicates a statistically significant p-value (below 0.01), implying a potentially important difference in gene expression between tumor and normal tissues. The y-axis represents the mean log2 (TPM + 1) values for gene expression levels. This transformation is commonly used in gene expression studies to stabilize variance across expression levels. At the stated cutoff, only EGFR and HSP90AA1 showed significant tumor-normal differences in the GEPIA2 analysis shown. HSP90AA1 was significantly upregulated and overexpressed in the TCGA_BRCA dataset. Additionally, TP53 was also overexpressed in the TCGA_BRCA dataset, but the difference was not significant (p > 0.05). In contrast, EGFR’s expression was significantly downregulated in this dataset. Moreover, STAT3 and SMAD3 expression was downregulated (p > 0.05) (Supplementary Figure 4). CTNNB1 showed a negligible change in expression in the TCGA_BRCA dataset (Supplementary Figure 3).

Heat Maps and Survival Analysis of Unique Genes

Using GEPIA2, a survival analysis was conducted by comparing gene expression levels identified in the survival heat map analysis with the TCGA_BRCA dataset (Supplementary Figure 4a). Among the six genes associated with breast cancer, HSP90AA1 and TP53 exhibited high expression levels in the BRCA dataset. Conversely, the remaining genes—CTNNB1, STAT3, SMAD3, and EGFR—demonstrated minimal expression in the BRCA dataset (Supplementary Figure 4a). A survival heatmap visually displays survival data, illustrating the relationship between specific variables (in this case, the six hub genes) and survival outcomes (such as overall survival time) across individuals or groups. The prognostic impact helps identify genes associated with improved or poorer survival, aiding the discovery of potential biomarkers for prognosis and treatment. Overall-survival analysis showed that the prognostic associations varied among the six hub genes. TP53 expression was significantly associated with poorer overall survival (HR = 1.4, p = 0.038), whereas the associations observed for HSP90AA1, CTNNB1, STAT3, SMAD3, and EGFR did not reach statistical significance under the analysis conditions used. Moreover, some genes exhibiting high expression levels and correlations with survival in BRCA patients included CTNNB1 (HR (Hazard ratio) = 0.94; p = 0.71), STAT3 (HR = 0.96; p = 0.82), SMAD3 (HR = 0.91; p = 0.58), and EGFR (HR = 0.9; p = 0.53). In contrast, the expression levels of TP53 (HR = 1.4, p = 0.038) and HSP90AA1 (HR = 1.3, p = 0.079) were associated with poorer prognoses and reduced survival rates among BRCA patients (Supplementary Figure 4b–g). The survival analysis suggested a potential association between higher TP53 expression and poorer overall survival (p = 0.038), whereas the association observed for HSP90AA1 was weaker and did not reach statistical significance. These findings should therefore be considered exploratory and require validation in independent cohorts (Supplementary Figure 4).

Molecular Docking and Visualization Analysis

Molecular docking was employed to predict the potential interactions between the selected P. longum phytochemicals and six breast cancer-associated hub proteins. The protein structures used for docking were obtained from the Protein Data Bank (PDB) and included 4MZI (TP53), 8Y0G (CTNNB1), 6NUQ (STAT3), 1MJS (SMAD3), 1M17 (EGFR), and 4BQG (HSP90AA1).[31–36] The predicted ligand docking score values for every hub gene are shown in Supplementary Table 7, in which the corresponding values, expressed in kcal/mol, represent the AutoDock Vina scores generated during the docking process and were used to rank the predicted binding poses. More negative Vina scores indicate more favorable predicted docking scores. Among the evaluated complexes, eleven protein–ligand interactions showed predicted binding affinities below −7 kcal/mol. These include HSP90AA1_Norcepharadione B (−10.9 kcal/mol), HSP90AA1_Aristolactam AII (−10.7 kcal/mol), HSP90AA1_Aristolodione (−10.3 kcal/mol), EGFR_Aristolodione (−9.1 kcal/mol), HSP90AA1_N-isobutyl decadienamide (−9 kcal/mol), EGFR_Norcepharadione B (−8.9 kcal/mol), EGFR_Aristolactam AII (−8.4 kcal/mol), STAT3_Aristolodione (−7.6 kcal/mol), HSP90AA1_Pellitorine (−7.5 kcal/mol), STAT3_Norcepharadione B (−7.2 kcal/mol), and TP53_Aristolodione (−7.1 kcal/mol). Figure 2 illustrates representative 3D and 2D interaction plots of five selected protein–ligand complexes showing strong predicted binding affinities.

Molecular docking results of key bioactive compounds of <em>P. longum</em> with breast cancer hub genes. (a) HSP90AA1_Norcepharadione B; (b) HSP90AA1_Aristolactam AII; (c) HSP90AA1_Aristolodione; (d) EGFR_Aristolodione; (e) HSP90AA1_N-isobutyl decadienamide.
Figure 2.
Molecular docking results of key bioactive compounds of P. longum with breast cancer hub genes. (a) HSP90AA1_Norcepharadione B; (b) HSP90AA1_Aristolactam AII; (c) HSP90AA1_Aristolodione; (d) EGFR_Aristolodione; (e) HSP90AA1_N-isobutyl decadienamide.

Piperine Assessment for Validation of Extracts

To evaluate the validation of different extracts of P. longum, the extracts were analyzed for the presence of piperine, one of the most abundant alkaloids found in P. longum fruits, using HPTLC (Figure 3a–d). As shown in Figure 3b–d, the HPTLC chromatogram indicated the presence of piperine in hydro-alcoholic extracts prepared by the Soxhlet method (lanes 1 and 2), aqueous extracts obtained through cold maceration (lanes 5 and 6), and dried fruit extract (lanes 7 and 8), all compared to piperine standards with an RF value of approximately 0.16. The aforementioned extracts were then tested for microbial contamination at the Department of Microbiology, AIIA. Subsequently, a 1 mg/mL stock solution of this extract was prepared in PBS (pH 7.2–7.4) and stored at −20°C for use in in vitro experiments (Figure 3e). Notably, piperine was used solely as a phytochemical marker for extract characterization and was not selected based on its network pharmacology ranking. In contrast, Norcepharadione B and Aristolactam AII were prioritized independently through the computational network pharmacology and molecular docking analyses based on their predicted interactions with breast cancer-associated targets. Thus, HPTLC detection of piperine provides chemical evidence for the characteristic composition of the extract but should not be interpreted as experimental validation of the predicted activities of Norcepharadione B, Aristolactam AII, or other computationally prioritized compounds.

Distribution of screening tests conducted.
Figure 3.
(a) Extract preparation. (b–d) HPTLC profile of standard and isolated piperine from different extraction methods and extract of P. longum dried fruits at 254nm (b), 366nm (c) and after derivatization (d) [1–2: Isolated Piperine from hydro-alcoholic Soxhlet method; 3–4: aqueous Soxhlet method; 5–6: cold maceration method; 7–8: P. longum dried fruit extract; 9–15: Piperine standard]. (e) Anti-microbial assessment of different extracts (A-Hydro-alcoholic extract by the Soxhlet method; B-aqueous extract by the Soxhlet method, and C-aqueous extract by the cold maceration method) on a Macconkey agar plate. (f) Line graph showing the effect of aqueous extract of P. longum on the growth of MCF-7 cell line using MTT assay.

Since we needed to treat the MCF-7 breast cancer cells with these extracts for subsequent experiments, we preferred to use the aqueous extract of P. longum prepared by cold maceration to minimize cell death caused by alcohol in the hydro-alcoholic extract.

Effect of P. longum Extract on MCF-7 MTT Signal

The effect of P. longum extract on MCF-7 MTT signal was analyzed after 24 hours of treatment using an MTT assay. The assay was conducted in both the extract-treated and untreated (control) groups. IC50 was reached at an extract concentration of 3.75 μg/mL (Figure 3f) after 24 hours post-treatment. Interestingly, increasing P. longum extract concentration was associated with a decrease in MCF-7 cell MTT signal; data are presented as mean ± standard deviation (SD) (Supplementary Table 8).

DISCUSSION

Network pharmacology provides a systematic framework for investigating the multi-target and multi-pathway effects of phytochemicals in complex diseases such as breast cancer. By integrating phytochemical information, disease-associated genes, PPI networks, pathway enrichment, and molecular docking, this approach can identify potential molecular targets and generate mechanistic hypotheses for further experimental validation.[37] In the present study, network pharmacology analysis identified several Piper longum-associated phytochemicals along with potential breast cancer-related targets, including TP53, CTNNB1, STAT3, SMAD3, EGFR, and HSP90AA1, which are involved in key biological processes regulating cell proliferation, survival, apoptosis, invasion, metastasis, and therapeutic resistance, thereby providing a computationally predicted basis for the potential anticancer activity of P. longum. These findings predicted P. longum-derived compounds and breast-cancer-associated targets that warrant direct experimental testing.

TP53 is among the most frequently altered genes in breast cancer and regulates cell-cycle progression, DNA damage responses, senescence, and apoptosis.[38] Similarly, CTNNB1, which encodes β-catenin, is a central component of Wnt signaling and has been associated with breast cancer progression and clinical outcome.[39] Constitutive activation of STAT3 contributes to breast cancer cell proliferation, survival, metastasis, and resistance to therapy, whereas SMAD3 overexpression has been associated with breast tumor growth and metastatic potential.[40–41] EGFR signaling is also involved in several downstream pathways, including JAK/STAT, PI3K/AKT, and RAS/RAF/MEK/ERK, which regulate cancer cell proliferation and survival and contribute to therapeutic resistance.[42] Furthermore, HSP90AA1 has been implicated in breast cancer biology and has potential diagnostic and prognostic relevance.[43] Thus, the network pharmacology analysis predicts that P. longum phytochemicals may modulate multiple oncogenic pathways rather than a single molecular target. These computational predictions require further experimental validation.

Functional enrichment analysis further supported this multi-target mechanism. The shared targets between P. longum phytochemicals and breast cancer were enriched in biological processes associated with growth-factor responses, responses to endogenous and chemical stimuli, and signal transduction. These findings are consistent with the established role of the tumor microenvironment in regulating cancer-cell metabolism, nutrient availability, and signaling. KEGG pathway analysis further identified enrichment of the PI3K–AKT, FOXO, microRNA, cancer-related, proteoglycan, and viral carcinogenesis pathways. Among these, the PI3K–AKT pathway is particularly relevant because it regulates proliferation, growth, survival, apoptosis, and migration and is frequently dysregulated in breast cancer. FOXO transcription factors are also closely linked to cellular stress responses, apoptosis, cancer-cell survival, and resistance to targeted therapies. In addition, microRNAs and proteoglycans may influence post-transcriptional gene regulation and extracellular-matrix-mediated processes involved in tumor invasion and metastasis.[44]

Molecular docking provided computational predictions regarding the potential interactions between selected P. longum phytochemicals and breast cancer-associated hub proteins. Among the evaluated interactions, Norcepharadione B showed the strongest predicted docking score toward HSP90AA1 (−10.9 kcal/mol), followed by Aristolactam AII (−10.7 kcal/mol) and Aristolodione (−10.3 kcal/mol). HSP90AA1 is a molecular chaperone that contributes to the stabilization and functional regulation of multiple oncogenic proteins.[45] Therefore, the favorable docking scores observed for these phytochemicals indicate that HSP90AA1 may represent a potential molecular target for future investigation. However, the present docking analysis does not demonstrate direct binding or modulation of HSP90AA1-mediated signaling, and these predicted interactions require biochemical and functional validation.

Importantly, the present study also reported experimental assessment of the effect of the aqueous P. longum extract on MCF-7 breast cancer cells. The growth-inhibitory effect was observed in the MTT assay. Previous studies have reported that piperlongumine, an individual constituent of P. longum, inhibits proliferation and induces cell-cycle arrest through ROS accumulation and suppression of IKKβ signaling. Although the precise mechanisms may differ, these published findings support the possibility that P. longum-derived phytochemicals influence cellular metabolism.[46] Additionally, piperine has also been reported to inhibit breast cancer cell growth and induce apoptosis, accompanied by caspase-3 activation.[4] Further, Prajapati et al.[5] explained that the combination of piperine and piperlongumine induces apoptosis in breast cancer cells by inhibiting STAT3 activation.[5] These findings are particularly relevant to the present network pharmacology results, in which STAT3 was predicted to be one of the major breast cancer-associated targets. Nevertheless, because the present study did not directly measure STAT3 activity or downstream apoptotic proteins, this mechanistic relationship should be considered a hypothesis requiring further validation. These observations are broadly consistent with the current findings and suggest that members of the Piperaceae family may exert anticancer activity through coordinated regulation of cell-cycle progression and apoptotic pathways. However, the differences in the specific cell-cycle phase affected by different Piper species and preparations highlight the importance of extract composition, extraction method, dose, and cellular context.

Strengths and Limitations

Taken together, the findings support a model in which the aqueous P. longum extract might exert anticancer activity through a multi-level mechanism. Network pharmacology predicted several cancer-associated molecular targets and pathways, while molecular docking prioritized putative compound-target interactions for further investigation. An in vitro study in MCF-7 cells demonstrated that the aqueous extract of P. longum significantly inhibits the MTT signal of the breast cancer cell line. These results suggest that the anticancer effects of P. longum may arise from the coordinated modulation of multiple signaling pathways involved in proliferation and survival.

The present study has several limitations that should be acknowledged. First, although the aqueous P. longum extract was characterized using HPTLC with piperine as a marker compound, comprehensive chemical standardization and quantitative estimation of the prioritized phytochemicals identified through network pharmacology, including Norcepharadione B and Aristolactam AII, were not performed. Therefore, the biological activity observed in the present study cannot be directly attributed to any individual constituent of the extract. Second, the in vitro experiments used only a single breast cancer cell line (MCF-7). Validation in additional breast cancer subtypes, including triple-negative and HER2-positive cell lines, would improve the generalizability of the findings. Third, the present study did not include a non-tumorigenic human breast epithelial cell line as a normal-cell comparator. Consequently, the selectivity of the extract toward cancer cells relative to normal cells could not be assessed. Finally, although the MTT assay demonstrated a significant reduction in cellular metabolic activity following treatment with the aqueous P. longum extract, plant-derived compounds may occasionally interfere with tetrazolium-based colorimetric assays through direct chemical reduction or intrinsic color. To minimize this possibility, the MTT findings should be complemented with independent cell-cycle and Annexin V/PI apoptosis assays, which consistently demonstrated cell-cycle arrest and increased apoptotic cell death. Nevertheless, additional orthogonal viability assays (such as ATP-based luminescence or live-cell imaging assays) would further strengthen these observations. An additional limitation of the present network pharmacology approach is that hub-gene prioritization was based on network topology analysis. Centrality measures, including degree, betweenness, and closeness centrality, preferentially identify highly connected and extensively studied genes within biological interaction networks. Consequently, these metrics do not necessarily identify the most disease-specific, biologically causal, or therapeutically druggable targets. Therefore, the hub genes identified in this study should be regarded as computationally prioritized candidates for further investigation rather than experimentally validated therapeutic targets. Future studies integrating functional genomics, target validation, and pharmacological experiments are needed to establish their biological significance and clinical relevance.

In brief, the computational predictions should not be interpreted as experimentally confirmed molecular mechanisms. Direct validation of the predicted interactions and pathways through target-specific approaches, including quantitative PCR, Western blotting, assessment of protein phosphorylation, and functional target inhibition or rescue experiments, will be warranted and will be carried out in our lab in the near future.

CONCLUSION AND IMPLICATIONS FOR TRANSLATION

The present study integrated network pharmacology and molecular docking to identify potential phytochemicals, molecular targets, and biological pathways that may contribute to the anticancer activity of Piper longum against breast cancer. The computational analyses generated hypotheses about compound–target interactions. At the same time, the in vitro experiments demonstrated that the aqueous P. longum extract reduces the MTT signal in MCF-7 cells. However, these findings should not be interpreted as evidence that specific phytochemicals directly interact with the predicted molecular targets or as proof of therapeutic efficacy. Instead, the present work provides a rational starting point for future compound-specific studies involving chemical standardization, target validation, mechanistic investigations, and comprehensive preclinical evaluation. Such studies will be essential to determine the biological relevance and translational potential of the identified phytochemicals before clinical application can be considered.

Acknowledgments

Shivam Singh thanks the Indian Council of Medical Research (ICMR; 5/13/58/2020/NCD-III) for providing the Project Research Scientist-II fellowship. We are also grateful to Mr Santosh Kumar, a PhD student in the Department of Biochemistry at AIIMS, New Delhi, India, for his valuable assistance with molecular docking and visualization analysis.

COMPLIANCE WITH ETHICAL STANDARDS

Conflicts of Interest: The authors declare no competing interests. Financial Disclosure: Nothing to declare. Funding/Supported: The study was financially supported by the ICMR (5/13/58/2020/NCD-III). Ethics Approval: Not Applicable. Use of Artificial Intelligence (AI)-Assisted Technology for Manuscript Preparation: The author(s) confirm that there was no use of AI-Assisted Technology for assisting in the writing or editing of the manuscript and no images were manipulated using AI. Disclaimer: None.

Key Messages

1) Piper longum shows promising anticancer potential because its bioactive phytochemicals may act on multiple breast cancer-related targets and signaling pathways. 2) Experimental findings support this potential, with the aqueous extract demonstrating growth-inhibitory and pro-apoptotic effects in MCF-7 breast cancer cells. 3) Findings provide a foundation for plant-derived, multi-target therapeutic development, but further compound-specific validation, mechanistic studies, and comprehensive preclinical evaluation are required before clinical potential can be established.

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Supplementary Figures

Flow diagram demonstrating the screening pipeline for compound selection.
Supplementary Figure 1:
Flow diagram demonstrating the screening pipeline for compound selection.
Top 23 GO terms and KEGG pathways associated with <em>P. longum</em> and breast cancer. (a) Cellular Components, (b) Molecular Functions, (c) Biological Processes, and (d) KEGG pathway.
Supplementary Figure 2:
Top 23 GO terms and KEGG pathways associated with P. longum and breast cancer. (a) Cellular Components, (b) Molecular Functions, (c) Biological Processes, and (d) KEGG pathway.
Box plots encode the six breast cancer-associated gene expression levels [(a) TP53, (b) CTNNB1, (c) STAT3,  (d) SMAD3, (e) EGFR, and (f) HSP90AA1] in BRCA compared with normal cells. Tumor tissues are marked in red color, and noncancerous or normal tissues are marked in grey color.
Supplementary Figure 3:
Box plots encode the six breast cancer-associated gene expression levels [(a) TP53, (b) CTNNB1, (c) STAT3, (d) SMAD3, (e) EGFR, and (f) HSP90AA1] in BRCA compared with normal cells. Tumor tissues are marked in red color, and noncancerous or normal tissues are marked in grey color.
Survival analysis demonstrating (a) the survival heat map representing the prognostic impacts of unique gene expression levels based on the TCGA_BRCA dataset. The heat map represents the hazard ratios on a log10 scale for the breast cancer-associated genes. Red color represents higher risks, and blue color indicates lower risks. The darkened rectangular frames indicate significant favorable and unfavorable results in prognostic analyses, and (b–g) breast cancer-associated unique genes and their prognostic value, as represented by overall survival analyses (Kaplan-Meier plots and log-rank tests) based on TCGA_BRCA using GEPIA2. The dashed lines denote upper and lower confidence intervals. (b) TP53, (c) CTNNB1, (d) STAT3, (e) SMAD3, (f) EGFR, and (g) HSP90AA1.
Supplementary Figure 4:
Survival analysis demonstrating (a) the survival heat map representing the prognostic impacts of unique gene expression levels based on the TCGA_BRCA dataset. The heat map represents the hazard ratios on a log10 scale for the breast cancer-associated genes. Red color represents higher risks, and blue color indicates lower risks. The darkened rectangular frames indicate significant favorable and unfavorable results in prognostic analyses, and (b–g) breast cancer-associated unique genes and their prognostic value, as represented by overall survival analyses (Kaplan-Meier plots and log-rank tests) based on TCGA_BRCA using GEPIA2. The dashed lines denote upper and lower confidence intervals. (b) TP53, (c) CTNNB1, (d) STAT3, (e) SMAD3, (f) EGFR, and (g) HSP90AA1.

Supplementary Tables

Supplementary Table 1: Extraction yields.
S. no. Extraction method Starting powder Dried extract Yield (%)
1 Cold aqueous 400 g 48.2 g 12.05
2 Soxhlet aqueous 400 g 39.8 g 9.95
3 Soxhlet hydroalcoholic 400 g 66.4 g 16.6
Supplementary Table 2: The list of compounds identified and their respective SMILES sequence from the fruit of P. longum.
S. no. Compounds in fruit Canonical/isomeric SMILES PubChem compounds (CIDs)
1 (-)-alpha-Cadinol CC1=C[C@H]2[C@@H](CC[C@@]([C@@H]2CC1)(C)O)C(C)C 10398656
2 (+)-alpha-Gurjunene C[C@H]1CC[C@H]2[C@H](C2(C)C)C3=C(CC[C@@H]13)C 15560275
3 (+)-beta-Phellandrene CC(C)[C@@H]1CCC(=C)C=C1 442484
4 (1R)-2-methyl-5-propan-2-ylbicyclo[3.1.0]hex-2-ene CC1=CC[C@]2([C@@H]1C2)C(C)C 637518
5 (E)-beta-ocimene CC(=CC/C=C(\\C)/C=C)C 5281553
6 (Z)-beta-Ocimene CC(=CC[C@@H]1[C@@](O1)(C)C=C)C 5320250
7 (Z)-gamma-bisabolene CC1=CC/C(=C(/C)\\CCC=C(C)C)/CC1 3033866
8 1-methylhexyl acetate CCCCCC(C)OC(=O)C 80018
9 1-pentadecene CCCCCCCCCCCCCC=C 25913
10 2-nonanone CCCCCCCC(=O)C 13187
11 2-phenylethanol C1=CC=C(C=C1)CCO 6054
12 2-tridecanone CCCCCCCCCCCC(=O)C 11622
13 2-undecanone CCCCCCCCCC(=O)C 8163
14 4’-methoxyacetophenone CC(=O)C1=CC=C(C=C1)OC 7476
15 5-[3-(1,3-benzodioxol-5-yl)-1,3,3a,4,6,6a-hexahydrofuro[3,4-c]furan-6-yl]-1,3-benzodioxole C1C2C(COC2C3=CC4=C(C=C3)OCO4)C(O1)C5=CC6=C(C=C5)OCO6 5204
16 9-Eicosyne CCCCCCCCCCC#CCCCCCCCC [1, 2] 557019
17 alpha-Eudesmol CC1=CCC[C@]2([C@H]1C[C@@H](CC2)C(C)(C)O)C 92762
18 alpha-Muurolene CC1=C[C@@H]2[C@H](CC1)C(=CC[C@H]2C(C)C)C 12306047
19 alpha-Phellandrene CC1=CCC(C=C1)C(C)C 7460
20 alpha-Pinene CC1=CCC2CC1C2(C)C 6654
21 alpha-Terpineol CC1=CCC(CC1)C(C)(C)O 17100
22 alpha-Terpinyl acetate CC1=CCC(CC1)C(C)(C)OC(=O)C 111037
23 Aristolactam AII COC1=C(C=C2C3=C1C4=CC=CC=C4C=C3NC2=O)O 148657
24 Aristolactam BII COC1=C(C2=C3C(=C1)C(=O)NC3=CC4=CC=CC=C42)OC 162739
25 Aristolodione CN1C2=CC3=CC=CC=C3C4=C2C(=CC(=C4OC)O)C(=O)C1=O 184116
26 Aristololactam COC1=CC=CC2=C3C4=C(C=C21)NC(=O)C4=CC5=C3OCO5 96710
27 beta-Caryophyllene C/C/1=C\\CCC(=C)[C@H]2CC([C@@H]2CC1)(C)C 5281515
28 beta-Cubebene CC(C)[C@@H]1CC[C@H]([C@H]2[C@]13[C@@H]2C(=C)CC3)C(C)C [1] 93081
29 beta-Elemene CC(=C)[C@@H]1CC[C@@]([C@@H](C1)C(=C)C)(C)C=C 6918391
30 beta-Eudesmol C[C@]12CCCC(=C)[C@@H]1C[C@@H](CC2)C(C)(C)O 91457
31 beta-Patchoulene CC1CCC2=C1CC3CCC2(C3(C)C)C 101731
32 beta-Pinene CC1(C2CCC(=C)C1C2)C 14896
33 Bornyl acetate CC(=O)O[C@@H]1C[C@@H]2CC[C@]1(C2(C)C)C 93009
34 Cadinane C[C@H]1CC[C@H]2[C@H](CC[C@H]([C@@H]2C1)C(C)C)C 9548708
35 Camphene CC1(C2CCC(C2)C1=C)C 6616
36 Caryophyllene oxide C[C@@]12CC[C@@H]3[C@H](CC3(C)C)C(=C)CC[C@H]1O2 1742210
37 Copaene CC1=CC[C@H]2[C@H]3[C@@H]1[C@@]2(CC[C@H]3C(C)C)C 12303902
38 Decanal CCCCCCCCCC=O 8175
39 Dehydropipernonaline C1CCN(CC1)C(=O)/C=C/C=C/CC/C=C/C2=CC3=C(C=C2)OCO3 6439947
40 delta-Cadinol CC1=C[C@H]2[C@@H](CC[C@@]([C@H]2CC1)(C)O)C(C)C 3084311
41 delta-Elemene CC(C)C1=C[C@@H]([C@@](CC1)(C)C=C)C(=C)C 12309449
42 Dihydrocarveol CC1CCC(CC1O)C(=C)C 12072
43 Dodecanal CCCCCCCCCCCC=O 8194
44 Eicosane CCCCCCCCCCCCCCCCCCCC 8222
45 Elemol CC(=C)[C@@H]1C[C@@H](CC[C@@]1(C)C=C)C(C)(C)O 92138
46 Eucalyptol CC1(C2CCC(O1)(CC2)C)C 2758
47 Fargesin COC1=C(C=C(C=C1)[C@H]2[C@H]3CO[C@@H]([C@H]3CO2)C4=CC5=C(C=C4)OCO5)OC 10926754
48 gamma-Elemene CC(=C1CC[C@]([C@H](C1)C(=C)C)(C)C=C)C 12309452
49 gamma-Muurolene CC1=C[C@@H]2[C@H](CC1)C(=C)CC[C@H]2C(C)C 12313020
50 Guineensine CC(C)CNC(=O)/C=C/C=C/CCCCCC/C=C/C1=CC2=C(C=C1)OCO2 6442405
51 Heneicosane CCCCCCCCCCCCCCCCCCCCC 12403
52 Heptadecane CCCCCCCCCCCCCCCCC 12398
53 Hexadecane CCCCCCCCCCCCCCCC 11006
54 Humulene C/C/1=C\\CC(/C=C/C/C(=C/CC1)/C)(C)C 5281520
55 Isobutyramide CC(C)C(=O)N 68424
56 Limonene CC1=CCC(CC1)C(=C)C 22311
57 Linalool CC(=CCCC(C)(C=C)O)C 6549
58 Myrcene CC(=CCCC(=C)C=C)C 31253
59 Nerolidol CC(=CCC/C(=C/CCC(C)(C=C)O)/C)C 5284507
60 Nonadecane CCCCCCCCCCCCCCCCCCC 12401
61 Norcepharadione B COC1=C(C2=C3C(=C1)C(=O)C(=O)NC3=CC4=CC=CC=C42)OC 189168
62 Octadecane CCCCCCCCCCCCCCCCCC 11635
63 p-Cymene CC1=CC=C(C=C1)C(C)C 7463
64 Pellitorine CCCCC/C=C/C=C/C(=O)NCC(C)C 5318516
65 Pentadecane CCCCCCCCCCCCCCC 12391
66 Piperidine C1CCNCC1 8082
67 Piperine C1CCN(CC1)C(=O)/C=C/C=C/C2=CC3=C(C=C2)OCO3 638024
68 Piperlongumine COC1=CC(=CC(=C1OC)OC)/C=C/C(=O)N2CCC=CC2=O 637858
69 Piperlonguminine CC(C)CNC(=O)/C=C/C=C/C1=CC2=C(C=C1)OCO2 5320621
70 Pipernonaline C1CCN(CC1)C(=O)/C=C/CCCC/C=C/C2=CC3=C(C=C2)OCO3 9974595
71 Piperoctadecalidine CCCC=CCCCCCCCCC=CC=CC(=O)N1CCCCC1 [1, 2] 177604078
72 Piperrolein B C1CCN(CC1)C(=O)CCCCCC/C=C/C2=CC3=C(C=C2)OCO3 21580213
73 Piperundecalidine C1CCN(CC1)C(=O)/C=C/C=C/CCCC/C=C/C2=CC3=C(C=C2)OCO3 44453654
74 Pluviatilol COC1=C(C=CC(=C1)[C@@H]2[C@@H]3CO[C@H]([C@@H]3CO2)C4=CC5=C(C=C4)OCO5)O 70695727
75 Terpinolene CC1=CCC(=C(C)C)CC1 11463
76 Tridecane CCCCCCCCCCCCC 12388
77 Zingiberene CC1=CC[C@@H](C=C1)[C@@H](C)CCC=C(C)C 92776
78 Longamide B C1C(N2C(=CC(=C2Br)Br)C(=O)N1)O 11602770
79 N-isobutyl decadienamide CCCCCC=CC=CC(=O)NCC(C)C 3009280
80 Sesamin C1[C@H]2[C@H](CO[C@@H]2C3=CC4=C(C=C3)OCO4)[C@H](O1)C5=CC6=C(C=C5)OCO6 72307
81 Tetrahydropiperine O=C(CCCCC1=CC(OCO2)=C2C=C1)N3CCCCC3 581676
82 Tetrahydropiperic acid OC(=O)CCCCC1=CC2=C(OCO2)C=C1 5321853
Supplementary Table 3: ADME properties of the selected phytochemicals of P. longum following the Lipinski’s rule of five and bioavailability score.
Name of the compound MW* MR† Rotatable bonds XLOGP3‡ H-bond acceptors H-bond donors Bioavailability score GI absorption# BBB penetration!
Norcepharadione B 307.3 90.02 2 3.16 4 1 0.55 High Yes
Piperine 285.3 85.47 4 3.46 3 0 0.55 High Yes
Aristolodione 307.3 90.45 1 3.02 4 1 0.55 High Yes
Aristolactam BII 279.3 83.75 2 3.28 3 1 0.55 High Yes
Dehydropipernonaline 339.4 104.23 7 4.7 3 0 0.55 High Yes
Piperlongumine 317.3 89.47 6 2.07 5 0 0.55 High Yes
Pluviatilol 356.4 92.45 3 2.48 6 1 0.55 High Yes
Aristololactam 293.3 83.32 1 3.12 4 1 0.55 High Yes
Fargesin 370.4 96.92 4 2.81 6 0 0.55 High Yes
Pellitorine 223.4 71.47 9 4.39 1 1 0.55 High Yes
Aristolactam AII 265.3 79.28 1 2.95 3 2 0.55 High Yes
Longamide 352 67.28 2 1.23 3 2 0.85 High Yes
Tetrahydropiperic acid 222.2 58.47 5 2.54 4 1 0.85 High Yes
Piperettine 311.4 94.61 5 4.11 3 0 0.55 High Yes
Asarinine 354.4 90 2 2.68 6 0 0.55 High Yes
Demethoxypiplartine 287.3 82.98 5 2.1 4 0 0.55 High Yes
N-isobutyl decadienamide 223.4 71.47 9 3.69 1 1 0.55 High Yes
Tetrahydro piperine 289.4 85.63 6 3.52 3 0 0.55 High Yes
Sesamin 354.4 90 2 2.68 6 0 0.55 High Yes

*Molecular weight;

†Number of rotatable bonds;

‡Partition coefficient;

#Gastrointestinal absorption; and Blood-Brain Barrier Penetration.

Supplementary Table 4: Complete list of target genes linked with P. longum and breast cancer.
S. no. Gene name Gene symbol HGNC ID
1 ATP binding cassette subfamily A member 1 ABCA1 HGNC:29
2 ATP binding cassette subfamily B member 1 ABCB1 HGNC:40
3 ATP binding cassette subfamily C member 1 (ABCC1 blood group) ABCC1 HGNC:51
4 ATP binding cassette subfamily C member 4 (PEL blood group) ABCC4 HGNC:55
5 ATP binding cassette subfamily G member 2 (JR blood group) ABCG2 HGNC:74
6 ABL proto-oncogene 1, non-receptor tyrosine kinase ABL1 HGNC:76
7 Abraxas 1, BRCA1 A complex subunit ABRAXAS1 HGNC:25829
8 Actin alpha 2, smooth muscle ACTA2 HGNC:130
9 Actin beta ACTB HGNC:132
10 Actin alpha cardiac muscle 1 ACTC1 HGNC:143
11 ADAM metallopeptidase domain 17 ADAM17 HGNC:195
12 Adrenoceptor beta 2 ADRB2 HGNC:286
13 Argonaute RISC catalytic component 2 AGO2 HGNC:3263
14 Aryl hydrocarbon receptor AHR HGNC:348
15 AKT serine/threonine kinase 1 AKT1 HGNC:391
16 AKT serine/threonine kinase 2 AKT2 HGNC:392
17 AKT serine/threonine kinase 3 AKT3 HGNC:393
18 Angiopoietin 1 ANGPT1 HGNC:484
19 Angiopoietin 2 ANGPT2 HGNC:485
20 APC regulator of Wnt signaling pathway APC HGNC:583
21 Androgen receptor AR HGNC:644
22 Amphiregulin AREG HGNC:651
23 AT-rich interaction domain 1A ARID1A HGNC:11110
24 ATM serine/threonine kinase ATM HGNC:795
25 ATPase copper transporting beta ATP7B HGNC:870
26 ATR checkpoint kinase ATR HGNC:882
27 Aurora kinase A AURKA HGNC:11393
28 AXL receptor tyrosine kinase AXL HGNC:905
29 BCL2 antagonist/killer 1 BAK1 HGNC:949
30 BRAF-activated non-protein coding RNA BANCR HGNC:43877
31 BRCA1 associated deubiquitinase 1 BAP1 HGNC:950
32 BRCA1 associated RING domain 1 BARD1 HGNC:952
33 BCL2 associated X, apoptosis regulator BAX HGNC:959
34 BCAR1 scaffold protein, Cas family member BCAR1 HGNC:971
35 BCAR3 adaptor protein, NSP family member BCAR3 HGNC:973
36 Brain enriched myelin associated protein 1 BCAS1 HGNC:974
37 BCL2 apoptosis regulator BCL2 HGNC:990
38 BCL2 like 1 BCL2L1 HGNC:992
39 Brain cytoplasmic RNA 1 BCYRN1 HGNC:1022
40 Baculoviral IAP repeat containing 3 BIRC3 HGNC:591
41 Baculoviral IAP repeat containing 5 BIRC5 HGNC:593
42 BLM RecQ like helicase BLM HGNC:1058
43 Bridge-like lipid transfer protein family member 2 BLTP2 HGNC:28960
44 BMI1 proto-oncogene, polycomb ring finger BMI1 HGNC:1066
45 Bone morphogenetic protein 4 BMP4 HGNC:1071
46 Bone morphogenetic protein 6 BMP6 HGNC:1073
47 Bone morphogenetic protein receptor type 1A BMPR1A HGNC:1076
48 B-Raf proto-oncogene, serine/threonine kinase BRAF HGNC:1097
49 BRCA1 DNA repair associated BRCA1 HGNC:1100
50 BRCA2 DNA repair associated BRCA2 HGNC:1101
51 BRCA1 interacting DNA helicase 1 BRIP1 HGNC:20473
52 BRMS1 transcriptional repressor and anoikis regulator BRMS1 HGNC:17262
53 BUB1 mitotic checkpoint serine/threonine kinase BUB1 HGNC:1148
54 BUB1 mitotic checkpoint serine/threonine kinase B BUB1B HGNC:1149
55 Calcium voltage-gated channel auxiliary subunit alpha2delta 1 CACNA2D1 HGNC:1399
56 Cancer susceptibility 15 CASC15 HGNC:28245
57 Caspase 10 CASP10 HGNC:1500
58 Caspase 3 CASP3 HGNC:1504
59 Caspase 8 CASP8 HGNC:1509
60 Caspase 9 CASP9 HGNC:1511
61 Caveolin 1 CAV1 HGNC:1527
62 Core-binding factor subunit beta CBFB HGNC:1539
63 Cbl proto-oncogene CBL HGNC:1541
64 C-C motif chemokine ligand 2 CCL2 HGNC:10618
65 Cyclin A2 CCNA2 HGNC:1578
66 Cyclin B1 CCNB1 HGNC:1579
67 Cyclin D1 CCND1 HGNC:1582
68 Cyclin D2 CCND2 HGNC:1583
69 Cyclin D3 CCND3 HGNC:1585
70 Cyclin E1 CCNE1 HGNC:1589
71 CD274 molecule CD274 HGNC:17635
72 CD3 gamma subunit of T-cell receptor complex CD3G HGNC:1675
73 CD44 molecule (IN blood group) CD44 HGNC:1681
74 CD82 molecule CD82 HGNC:6210
75 Cell division cycle 25A CDC25A HGNC:1725
76 Cell division cycle 73 CDC73 HGNC:16783
77 Cadherin 1 CDH1 HGNC:1748
78 Cadherin 3 CDH3 HGNC:1762
79 Cyclin dependent kinase 1 CDK1 HGNC:1722
80 Cyclin dependent kinase 2 CDK2 HGNC:1771
81 Cyclin dependent kinase 4 CDK4 HGNC:1773
82 Cyclin dependent kinase 6 CDK6 HGNC:1777
83 Cyclin dependent kinase inhibitor 1A CDKN1A HGNC:1784
84 Cyclin dependent kinase inhibitor 1B CDKN1B HGNC:1785
85 Cyclin dependent kinase inhibitor 1C CDKN1C HGNC:1786
86 Cyclin dependent kinase inhibitor 2A CDKN2A HGNC:1787
87 Cyclin dependent kinase inhibitor 2B CDKN2B HGNC:1788
88 Cyclin dependent kinase inhibitor 2C CDKN2C HGNC:1789
89 Cyclin dependent kinase inhibitor 3 CDKN3 HGNC:1791
90 CEA cell adhesion molecule 5 CEACAM5 HGNC:1817
91 CCAAT enhancer binding protein alpha CEBPA HGNC:1833
92 CF transmembrane conductance regulator CFTR HGNC:1884
93 Checkpoint kinase 1 CHEK1 HGNC:1925
94 Checkpoint kinase 2 CHEK2 HGNC:16627
95 Cholinergic receptor nicotinic alpha 7 subunit CHRNA7 HGNC:1960
96 CDC28 protein kinase regulatory subunit 1B CKS1B HGNC:19083
97 Collagen type III alpha 1 chain COL3A1 HGNC:2201
98 Catechol-O-methyltransferase COMT HGNC:2228
99 cAMP responsive element binding protein 1 CREB1 HGNC:2345
100 CREB binding lysine acetyltransferase CREBBP HGNC:2348
101 Colorectal neoplasia differentially expressed CRNDE HGNC:37078
102 Colony stimulating factor 1 CSF1 HGNC:2432
103 Colony stimulating factor 1 receptor CSF1R HGNC:2433
104 Colony stimulating factor 2 CSF2 HGNC:2434
105 CCCTC-binding factor CTCF HGNC:13723
106 Cytotoxic T-lymphocyte associated protein 4 CTLA4 HGNC:2505
107 Catenin alpha 1 CTNNA1 HGNC:2509
108 Catenin beta 1 CTNNB1 HGNC:2514
109 Cathepsin D CTSD HGNC:2529
110 C-X-C motif chemokine ligand 12 CXCL12 HGNC:10672
111 C-X-C motif chemokine ligand 8 CXCL8 HGNC:6025
112 C-X-C motif chemokine receptor 4 CXCR4 HGNC:2561
113 Cytochrome c, somatic CYCS HGNC:19986
114 CYLD lysine 63 deubiquitinase CYLD HGNC:2584
115 Cytochrome P450 family 1 subfamily A member 1 CYP1A1 HGNC:2595
116 Cytochrome P450 family 1 subfamily B member 1 CYP1B1 HGNC:2597
117 Cytochrome P450 family 2 subfamily D member 6 (gene/pseudogene) CYP2D6 HGNC:2625
118 Cytoskeleton regulator RNA CYTOR HGNC:28717
119 DCC netrin 1 receptor DCC HGNC:2701
120 Dynactin subunit 5 DCTN5 HGNC:24594
121 Damage specific DNA binding protein 2 DDB2 HGNC:2718
122 Discoidin domain receptor tyrosine kinase 1 DDR1 HGNC:2730
123 DEAD-box helicase 5 DDX5 HGNC:2746
124 Dihydrofolate reductase DHFR HGNC:2861
125 Dicer 1, ribonuclease III DICER1 HGNC:17098
126 DIS3 like 3'-5' exoribonuclease 2 DIS3L2 HGNC:28648
127 DLC1 Rho GTPase activating protein DLC1 HGNC:2897
128 DNA methyltransferase 1 DNMT1 HGNC:2976
129 DNA methyltransferase 3 alpha DNMT3A HGNC:2978
130 DNA methyltransferase 3 beta DNMT3B HGNC:2979
131 Dihydropyrimidine dehydrogenase DPYD HGNC:3012
132 Drosha ribonuclease III DROSHA HGNC:17904
133 Desmoglein 2 DSG2 HGNC:3049
134 Desmoplakin DSP HGNC:3052
135 E2F transcription factor 1 E2F1 HGNC:3113
136 E2F transcription factor 4 E2F4 HGNC:3118
137 Ephrin A3 EFNA3 HGNC:3223
138 Epidermal growth factor EGF HGNC:3229
139 Epidermal growth factor receptor EGFR HGNC:3236
140 ELAV like RNA binding protein 1 ELAVL1 HGNC:3312
141 Endoglin ENG HGNC:3349
142 EP300 lysine acetyltransferase EP300 HGNC:3373
143 Epithelial cell adhesion molecule EPCAM HGNC:11529
144 EPH receptor A2 EPHA2 HGNC:3386
145 EPH receptor B2 EPHB2 HGNC:3393
146 EPH receptor B4 EPHB4 HGNC:3395
147 erb-b2 receptor tyrosine kinase 2 ERBB2 HGNC:3430
148 erb-b2 receptor tyrosine kinase 3 ERBB3 HGNC:3431
149 erb-b2 receptor tyrosine kinase 4 ERBB4 HGNC:3432
150 ERCC excision repair 1, endonuclease non-catalytic subunit ERCC1 HGNC:3433
151 ERCC excision repair 2, TFIIH core complex helicase subunit ERCC2 HGNC:3434
152 ERCC excision repair 3, TFIIH core complex helicase subunit ERCC3 HGNC:3435
153 ERCC excision repair 4, endonuclease catalytic subunit ERCC4 HGNC:3436
154 ERCC excision repair 5, endonuclease ERCC5 HGNC:3437
155 ERCC excision repair 6, chromatin remodeling factor ERCC6 HGNC:3438
156 Endogenous retrovirus group 48 member 1, envelope ERVH48-1 HGNC:17216
157 Estrogen receptor 2 ESR2 HGNC:3468
158 ETS proto-oncogene 1, transcription factor ETS1 HGNC:3488
159 Exocyst complex component 2 EXOC2 HGNC:24968
160 Exostosin glycosyltransferase 1 EXT1 HGNC:3512
161 Enhancer of zeste 2 polycomb repressive complex 2 subunit EZH2 HGNC:3527
162 FA complementation group A FANCA HGNC:3582
163 FA complementation group B FANCB HGNC:3583
164 FA complementation group C FANCC HGNC:3584
165 FA complementation group D2 FANCD2 HGNC:3585
166 FA complementation group I FANCI HGNC:25568
167 FA complementation group L FANCL HGNC:20748
168 Fas cell surface death receptor FAS HGNC:11920
169 Fas ligand FASLG HGNC:11936
170 Fatty acid synthase FASN HGNC:3594
171 Fibrillin 1 FBN1 HGNC:3603
172 F-box protein 32 FBXO32 HGNC:16731
173 F-box and WD repeat domain containing 7 FBXW7 HGNC:16712
174 Fibroblast growth factor 2 FGF2 HGNC:3676
175 Fibroblast growth factor receptor 1 FGFR1 HGNC:3688
176 Fibroblast growth factor receptor 2 FGFR2 HGNC:3689
177 Fibroblast growth factor receptor 3 FGFR3 HGNC:3690
178 Fibroblast growth factor receptor 4 FGFR4 HGNC:3691
179 Fumarate hydratase FH HGNC:3700
180 Fragile histidine triad diadenosine triphosphatase FHIT HGNC:3701
181 Folliculin FLCN HGNC:27310
182 Fms related receptor tyrosine kinase 1 FLT1 HGNC:3763
183 Fms related receptor tyrosine kinase 3 FLT3 HGNC:3765
184 Fms related receptor tyrosine kinase 4 FLT4 HGNC:3767
185 Fibronectin 1 FN1 HGNC:3778
186 Fos proto-oncogene, AP-1 transcription factor subunit FOS HGNC:3796
187 Forkhead box A1 FOXA1 HGNC:5021
188 Forkhead box M1 FOXM1 HGNC:3818
189 Forkhead box O1 FOXO1 HGNC:3819
190 Forkhead box O3 FOXO3 HGNC:3821
191 Polypeptide N-acetylgalactosaminyltransferase 12 GALNT12 HGNC:19877
192 Growth arrest specific 5 GAS5 HGNC:16355
193 GATA binding protein 2 GATA2 HGNC:4171
194 GATA binding protein 3 GATA3 HGNC:4172
195 Glutaminase GLS HGNC:4331
196 GNAS complex locus GNAS HGNC:4392
197 Gonadotropin releasing hormone 1 GNRH1 HGNC:4419
198 Glypican 3 GPC3 HGNC:4451
199 G protein-coupled estrogen receptor 1 GPER1 HGNC:4485
200 G protein signaling modulator 2 GPSM2 HGNC:29501
201 Growth factor receptor bound protein 2 GRB2 HGNC:4566
202 Growth regulating estrogen receptor binding 1 GREB1 HGNC:24885
203 Gremlin 1, DAN family BMP antagonist GREM1 HGNC:2001
204 Glycogen synthase kinase 3 beta GSK3B HGNC:4617
205 Glutathione S-transferase mu 1 GSTM1 HGNC:4632
206 Glutathione S-transferase pi 1 GSTP1 HGNC:4638
207 Glutathione S-transferase theta 1 GSTT1 HGNC:4641
208 H19 imprinted maternally expressed transcript H19 HGNC:4713
209 HOXD antisense growth-associated long non-coding RNA HAGLR HGNC:43755
210 Histone deacetylase 1 HDAC1 HGNC:4852
211 Histone deacetylase 4 HDAC4 HGNC:14063
212 Homeostatic iron regulator HFE HGNC:4886
213 Hepatocyte growth factor HGF HGNC:4893
214 Hypoxia inducible factor 1 subunit alpha HIF1A HGNC:4910
215 HIF1A antisense RNA 2 HIF1A-AS2 HGNC:43015
216 High mobility group AT-hook 2 HMGA2 HGNC:5009
217 Hyaluronan mediated motility receptor HMMR HGNC:5012
218 HNF1 homeobox A HNF1A HGNC:11621
219 HOX transcript antisense RNA HOTAIR HGNC:33510
220 HOXA cluster antisense RNA 2 HOXA-AS2 HGNC:43745
221 Homeobox B13 HOXB13 HGNC:5112
222 HR lysine demethylase and nuclear receptor corepressor HR HGNC:5172
223 HRas proto-oncogene, GTPase HRAS HGNC:5173
224 Hydroxysteroid 17-beta dehydrogenase 1 HSD17B1 HGNC:5210
225 Heat shock protein 90 alpha family class A member 1 HSP90AA1 HGNC:5253
226 Heat shock protein family B (small) member 1 HSPB1 HGNC:5246
227 Intercellular adhesion molecule 1 ICAM1 HGNC:5344
228 Isocitrate dehydrogenase (NADP(+)) 1 IDH1 HGNC:5382
229 Isocitrate dehydrogenase (NADP(+)) 2 IDH2 HGNC:5383
230 Interferon gamma IFNG HGNC:5438
231 Insulin like growth factor 1 receptor IGF1R HGNC:5465
232 Insulin like growth factor 2 IGF2 HGNC:5466
233 Insulin like growth factor 2 receptor IGF2R HGNC:5467
234 Insulin like growth factor binding protein 3 IGFBP3 HGNC:5472
235 Interleukin 10 IL10 HGNC:5962
236 Interleukin 12B IL12B HGNC:5970
237 Interleukin 1 beta IL1B HGNC:5992
238 Interleukin 1 receptor antagonist IL1RN HGNC:6000
239 Interleukin 2 IL2 HGNC:6001
240 Interleukin 6 IL6 HGNC:6018
241 Interleukin 7 receptor IL7R HGNC:6024
242 Inosine monophosphate dehydrogenase 1 IMPDH1 HGNC:6052
243 Insulin INS HGNC:6081
244 Interferon regulatory factor 1 IRF1 HGNC:6116
245 Insulin receptor substrate 1 IRS1 HGNC:6125
246 Itchy E3 ubiquitin protein ligase ITCH HGNC:13890
247 Integrin subunit beta 1 ITGB1 HGNC:6153
248 Janus kinase 1 JAK1 HGNC:6190
249 Janus kinase 2 JAK2 HGNC:6192
250 Jun proto-oncogene, AP-1 transcription factor subunit JUN HGNC:6204
251 KCNQ1 opposite strand/antisense transcript 1 KCNQ1OT1 HGNC:6295
252 Lysine demethylase 4B KDM4B HGNC:29136
253 Lysine demethylase 6A KDM6A HGNC:12637
254 Kinase insert domain receptor KDR HGNC:6307
255 Kelch like ECH associated protein 1 KEAP1 HGNC:23177
256 KiSS-1 metastasis suppressor KISS1 HGNC:6341
257 KIT proto-oncogene, receptor tyrosine kinase KIT HGNC:6342
258 KIT ligand KITLG HGNC:6343
259 kinesin light chain 1 KLC1 HGNC:6387
260 KLF3 antisense RNA 1 KLF3-AS1 HGNC:25796
261 KLF transcription factor 4 KLF4 HGNC:6348
262 KLF transcription factor 6 KLF6 HGNC:2235
263 Kallikrein related peptidase 3 KLK3 HGNC:6364
264 Lysine methyltransferase 2A KMT2A HGNC:7132
265 Lysine methyltransferase 2C KMT2C HGNC:13726
266 Lysine methyltransferase 2D KMT2D HGNC:7133
267 KRas proto-oncogene, GTPase KRAS HGNC:6407
268 Keratin 18 KRT18 HGNC:6430
269 Keratin 19 KRT19 HGNC:6436
270 Keratin 20 KRT20 HGNC:20412
271 Keratin 5 KRT5 HGNC:6442
272 Keratin 7 KRT7 HGNC:6445
273 Keratin 8 KRT8 HGNC:6446
274 Lymphocyte cytosolic protein 1 LCP1 HGNC:6528
275 Low density lipoprotein receptor LDLR HGNC:6547
276 Lymphoid enhancer binding factor 1 LEF1 HGNC:6551
277 Leptin LEP HGNC:6553
278 Leptin receptor LEPR HGNC:6554
279 Long independently transcribed non-coding RNA 472 LINC00472 HGNC:21380
280 Long independently transcribed non-coding RNA 1116 LINC01116 HGNC:49259
281 LDL receptor related protein 1B LRP1B HGNC:6693
282 Lung cancer associated transcript 1 LUCAT1 HGNC:48498
283 Metastasis associated lung adenocarcinoma transcript 1 MALAT1 HGNC:29665
284 Mitogen-activated protein kinase kinase 1 MAP2K1 HGNC:6840
285 Mitogen-activated protein kinase kinase 2 MAP2K2 HGNC:6842
286 Mitogen-activated protein kinase kinase 4 MAP2K4 HGNC:6844
287 Mitogen-activated protein kinase kinase kinase 1 MAP3K1 HGNC:6848
288 Mitogen-activated protein kinase kinase kinase 6 MAP3K6 HGNC:6858
289 Mitogen-activated protein kinase 1 MAPK1 HGNC:6871
290 Mitogen-activated protein kinase 10 MAPK10 HGNC:6872
291 Mitogen-activated protein kinase 14 MAPK14 HGNC:6876
292 Mitogen-activated protein kinase 8 MAPK8 HGNC:6881
293 MYC associated transcriptional regulator X MAX HGNC:6913
294 Melanocortin 1 receptor MC1R HGNC:6929
295 Melanocortin 4 receptor MC4R HGNC:6932
296 MCL1 apoptosis regulator, BCL2 family member MCL1 HGNC:6943
297 MDM2 proto-oncogene MDM2 HGNC:6973
298 MDM4 regulator of p53 MDM4 HGNC:6974
299 Mediator complex subunit 1 MED1 HGNC:9234
300 Mediator complex subunit 12 MED12 HGNC:11957
301 Maternally expressed 3 MEG3 HGNC:14575
302 Maternal embryonic leucine zipper kinase MELK HGNC:16870
303 Menin 1 MEN1 HGNC:7010
304 MET proto-oncogene, receptor tyrosine kinase MET HGNC:7029
305 O-6-methylguanine-DNA methyltransferase MGMT HGNC:7059
306 Myocardial infarction associated transcript MIAT HGNC:33425
307 microRNA 106b MIR106B HGNC:31495
308 microRNA 10b MIR10B HGNC:31498
309 microRNA 125a MIR125A HGNC:31505
310 microRNA 126 MIR126 HGNC:31508
311 microRNA 127 MIR127 HGNC:31509
312 microRNA 132 MIR132 HGNC:31516
313 microRNA 135b MIR135B HGNC:31760
314 microRNA 139 MIR139 HGNC:31526
315 microRNA 141 MIR141 HGNC:31528
316 microRNA 143 MIR143 HGNC:31530
317 microRNA 146a MIR146A HGNC:31533
318 microRNA 149 MIR149 HGNC:31536
319 microRNA 15a MIR15A HGNC:31543
320 microRNA 15b MIR15B HGNC:31544
321 microRNA 17 MIR17 HGNC:31547
322 microRNA 182 MIR182 HGNC:31553
323 microRNA 183 MIR183 HGNC:31554
324 microRNA 192 MIR192 HGNC:31562
325 microRNA 196b MIR196B HGNC:31790
326 microRNA 200a MIR200A HGNC:31578
327 microRNA 200b MIR200B HGNC:31579
328 microRNA 200c MIR200C HGNC:31580
329 microRNA 20a MIR20A HGNC:31577
330 microRNA 21 MIR21 HGNC:31586
331 microRNA 210 MIR210 HGNC:31587
332 microRNA 22 MIR22 HGNC:31599
333 microRNA 221 MIR221 HGNC:31601
334 microRNA 24-1 MIR24-1 HGNC:31607
335 microRNA 25 MIR25 HGNC:31609
336 microRNA 30a MIR30A HGNC:31624
337 microRNA 30b MIR30B HGNC:31625
338 microRNA 30e MIR30E HGNC:31629
339 microRNA 320a MIR320A HGNC:31632
340 microRNA 342 MIR342 HGNC:31778
341 microRNA 34a MIR34A HGNC:31635
342 microRNA 34b MIR34B HGNC:31636
343 microRNA 34c MIR34C HGNC:31637
344 microRNA 424 MIR424 HGNC:31881
345 microRNA 425 MIR425 HGNC:31882
346 microRNA 494 MIR494 HGNC:32084
347 microRNA 497 MIR497 HGNC:32088
348 microRNA 542 MIR542 HGNC:32534
349 MIR7-3 host gene MIR7-3HG HGNC:30049
350 microRNA 92a-1 MIR92A1 HGNC:31643
351 microRNA 93 MIR93 HGNC:31645
352 microRNA 96 MIR96 HGNC:31648
353 microRNA 98 MIR98 HGNC:31649
354 microRNA 99a MIR99A HGNC:31650
355 microRNA let-7b MIRLET7B HGNC:31479
356 microRNA let-7d MIRLET7D HGNC:31481
357 microRNA let-7e MIRLET7E HGNC:31482
358 microRNA let-7g MIRLET7G HGNC:31485
359 Melanocyte inducing transcription factor MITF HGNC:7105
360 Marker of proliferation Ki-67 MKI67 HGNC:7107
361 MutL homolog 1 MLH1 HGNC:7127
362 MutL homolog 3 MLH3 HGNC:7128
363 Matrix metallopeptidase 1 MMP1 HGNC:7155
364 Matrix metallopeptidase 14 MMP14 HGNC:7160
365 Matrix metallopeptidase 2 MMP2 HGNC:7166
366 Matrix metallopeptidase 7 MMP7 HGNC:7174
367 Matrix metallopeptidase 9 MMP9 HGNC:7176
368 MRE11 double strand break repair nuclease MRE11 HGNC:7230
369 MutS homolog 2 MSH2 HGNC:7325
370 MutS homolog 6 MSH6 HGNC:7329
371 Macrophage scavenger receptor 1 MSR1 HGNC:7376
372 Metastasis associated 1 MTA1 HGNC:7410
373 Methylenetetrahydrofolate reductase MTHFR HGNC:7436
374 Mechanistic target of rapamycin kinase MTOR HGNC:3942
375 5-methyltetrahydrofolate-homocysteine methyltransferase MTR HGNC:7468
376 Mucin 1, cell surface associated MUC1 HGNC:7508
377 Mucin 16, cell surface associated MUC16 HGNC:15582
378 MAX interactor 1, dimerization protein MXI1 HGNC:7534
379 MYB proto-oncogene, transcription factor MYB HGNC:7545
380 MYC proto-oncogene, bHLH transcription factor MYC HGNC:7553
381 N-acetyltransferase 2 NAT2 HGNC:7646
382 Nibrin NBN HGNC:7652
383 Nuclear receptor coactivator 3 NCOA3 HGNC:7670
384 Nuclear receptor corepressor 1 NCOR1 HGNC:7672
385 Nuclear receptor corepressor 2 NCOR2 HGNC:7673
386 Nuclear paraspeckle assembly transcript 1 NEAT1 HGNC:30815
387 NIMA related kinase 2 NEK2 HGNC:7745
388 neurofibromin 1 NF1 HGNC:7765
389 NFE2 like bZIP transcription factor 2 NFE2L2 HGNC:7782
390 Nuclear factor kappa B subunit 1 NFKB1 HGNC:7794
391 NFKB inhibitor alpha NFKBIA HGNC:7797
392 NK2 homeobox 1 NKX2-1 HGNC:11825
393 NME/NM23 nucleoside diphosphate kinase 1 NME1 HGNC:7849
394 NNT antisense RNA 1 NNT-AS1 HGNC:49005
395 Nitric oxide synthase 2 NOS2 HGNC:7873
396 Notch receptor 1 NOTCH1 HGNC:7881
397 Notch receptor 2 NOTCH2 HGNC:7882
398 Notch receptor 3 NOTCH3 HGNC:7883
399 Nucleophosmin 1 NPM1 HGNC:7910
400 NAD(P)H quinone dehydrogenase 1 NQO1 HGNC:2874
401 N-ribosyldihydronicotinamide:quinone dehydrogenase 2 NQO2 HGNC:7856
402 Nuclear receptor subfamily 3 group C member 1 NR3C1 HGNC:7978
403 NRAS proto-oncogene, GTPase NRAS HGNC:7989
404 Neuregulin 1 NRG1 HGNC:7997
405 Nth like DNA glycosylase 1 NTHL1 HGNC:8028
406 Neurotrophic receptor tyrosine kinase 1 NTRK1 HGNC:8031
407 Neurotrophic receptor tyrosine kinase 2 NTRK2 HGNC:8032
408 Neurotrophic receptor tyrosine kinase 3 NTRK3 HGNC:8033
409 Ornithine decarboxylase 1 ODC1 HGNC:8109
410 8-oxoguanine DNA glycosylase OGG1 HGNC:8125
411 Phenylalanine hydroxylase PAH HGNC:8582
412 p21 (RAC1) activated kinase 1 PAK1 HGNC:8590
413 Partner and localizer of BRCA2 PALB2 HGNC:26144
414 Palladin, cytoskeletal associated protein PALLD HGNC:17068
415 Poly(ADP-ribose) polymerase 1 PARP1 HGNC:270
416 Polybromo 1 PBRM1 HGNC:30064
417 Polycomb group ring finger 2 PCGF2 HGNC:12929
418 Proliferating cell nuclear antigen PCNA HGNC:8729
419 Programmed cell death 1 PDCD1 HGNC:8760
420 Platelet derived growth factor subunit B PDGFB HGNC:8800
421 Platelet derived growth factor receptor alpha PDGFRA HGNC:8803
422 Prohibitin 1 PHB1 HGNC:8912
423 Paired like homeobox 2B PHOX2B HGNC:9143
424 Phosphatidylinositol-4,5-bisphosphate 3-kinase catalytic subunit alpha PIK3CA HGNC:8975
425 Phosphatidylinositol-4,5-bisphosphate 3-kinase catalytic subunit beta PIK3CB HGNC:8976
426 Phosphatidylinositol-4,5-bisphosphate 3-kinase catalytic subunit delta PIK3CD HGNC:8977
427 Phosphatidylinositol-4,5-bisphosphate 3-kinase catalytic subunit gamma PIK3CG HGNC:8978
428 Phosphoinositide-3-kinase regulatory subunit 1 PIK3R1 HGNC:8979
429 Phosphoinositide-3-kinase regulatory subunit 2 PIK3R2 HGNC:8980
430 Pyruvate kinase M1/2 PKM HGNC:9021
431 Plasminogen activator, urokinase PLAU HGNC:9052
432 Plasminogen activator, urokinase receptor PLAUR HGNC:9053
433 Polo like kinase 1 PLK1 HGNC:9077
434 PML nuclear body scaffold PML HGNC:9113
435 PMS1 homolog 1, mismatch repair system component PMS1 HGNC:9121
436 PMS1 homolog 2, mismatch repair system component PMS2 HGNC:9122
437 DNA polymerase delta 1, catalytic subunit POLD1 HGNC:9175
438 DNA polymerase epsilon, catalytic subunit POLE HGNC:9177
439 Protection of telomeres 1 POT1 HGNC:17284
440 POU class 5 homeobox 1 POU5F1 HGNC:9221
441 Peroxisome proliferator activated receptor gamma PPARG HGNC:9236
442 Protein phosphatase, Mg2+/Mn2+ dependent 1D PPM1D HGNC:9277
443 Protein phosphatase, Mg2+/Mn2+ dependent 1L PPM1L HGNC:16381
444 Protein phosphatase 2 scaffold subunit Abeta PPP2R1B HGNC:9303
445 Protein phosphatase 2 regulatory subunit Balpha PPP2R2A HGNC:9304
446 Protein regulator of cytokinesis 1 PRC1 HGNC:9341
447 Protein kinase cAMP-activated catalytic subunit alpha PRKACA HGNC:9380
448 Protein kinase cAMP-dependent type I regulatory subunit alpha PRKAR1A HGNC:9388
449 Protein kinase C alpha PRKCA HGNC:9393
450 Protein kinase, DNA-activated, catalytic subunit PRKDC HGNC:9413
451 Parkin RBR E3 ubiquitin protein ligase PRKN HGNC:8607
452 Prolactin receptor PRLR HGNC:9446
453 Phosphatase and tensin homolog PTEN HGNC:9588
454 Prostaglandin F receptor PTGFR HGNC:9600
455 Prostaglandin-endoperoxide synthase 2 PTGS2 HGNC:9605
456 Parathyroid hormone like hormone PTHLH HGNC:9607
457 Protein tyrosine kinase 2 PTK2 HGNC:9611
458 Protein tyrosine phosphatase non-receptor type 11 PTPN11 HGNC:9644
459 Protein tyrosine phosphatase non-receptor type 3 PTPN3 HGNC:9655
460 RAB, member of RAS oncogene family like 3 RABL3 HGNC:18072
461 Rac family small GTPase 1 RAC1 HGNC:9801
462 RAD50 double strand break repair protein RAD50 HGNC:9816
463 RAD51 recombinase RAD51 HGNC:9817
464 RAD51 paralog B RAD51B HGNC:9822
465 RAD51 paralog C RAD51C HGNC:9820
466 RAD54 like RAD54L HGNC:9826
467 Raf-1 proto-oncogene, serine/threonine kinase RAF1 HGNC:9829
468 Retinoic acid receptor alpha RARA HGNC:9864
469 Ras association domain family member 1 RASSF1 HGNC:9882
470 RB transcriptional corepressor 1 RB1 HGNC:9884
471 RB1 inducible coiled-coil 1 RB1CC1 HGNC:15574
472 RB binding protein 8, endonuclease RBBP8 HGNC:9891
473 Reversion inducing cysteine rich protein with kazal motifs RECK HGNC:11345
474 RecQ like helicase RECQL HGNC:9948
475 RecQ like helicase 4 RECQL4 HGNC:9949
476 RELA proto-oncogene, NF-kB subunit RELA HGNC:9955
477 RE1 silencing transcription factor REST HGNC:9966
478 Ret proto-oncogene RET HGNC:9967
479 Rhomboid 5 homolog 2 RHBDF2 HGNC:20788
480 Ras homolog family member A RHOA HGNC:667
481 Rho related BTB domain containing 2 RHOBTB2 HGNC:18756
482 RAD50 interactor 1 RINT1 HGNC:21876
483 Receptor interacting serine/threonine kinase 1 RIPK1 HGNC:10019
484 Rhabdomyosarcoma 2 associated transcript RMST HGNC:29893
485 Ribonuclease L RNASEL HGNC:10050
486 Ring finger protein 43 RNF43 HGNC:18505
487 Ribosomal protein S6 kinase B1 RPS6KB1 HGNC:10436
488 RUNX family transcription factor 1 RUNX1 HGNC:10471
489 S100 calcium binding protein A4 S100A4 HGNC:10494
490 Succinate dehydrogenase complex flavoprotein subunit A SDHA HGNC:10680
491 Succinate dehydrogenase complex assembly factor 2 SDHAF2 HGNC:26034
492 Succinate dehydrogenase complex iron sulfur subunit B SDHB HGNC:10681
493 Succinate dehydrogenase complex subunit C SDHC HGNC:10682
494 Succinate dehydrogenase complex subunit D SDHD HGNC:10683
495 Septin 9 SEPTIN9 HGNC:7323
496 Serpin family E member 1 SERPINE1 HGNC:8583
497 SET domain containing 2, histone lysine methyltransferase SETD2 HGNC:18420
498 SHC adaptor protein 1 SHC1 HGNC:10840
499 S-phase kinase associated protein 2 SKP2 HGNC:10901
500 Solute carrier family 19 member 1 SLC19A1 HGNC:10937
501 Solute carrier family 2 member 1 SLC2A1 HGNC:11005
502 Solute carrier family 39 member 6 SLC39A6 HGNC:18607
503 SLX4 structure-specific endonuclease subunit SLX4 HGNC:23845
504 SMAD family member 2 SMAD2 HGNC:6768
505 SMAD family member 3 SMAD3 HGNC:6769
506 SMAD family member 4 SMAD4 HGNC:6770
507 SMAD family member 7 SMAD7 HGNC:6773
508 SWI/SNF related BAF chromatin remodeling complex subunit ATPase 4 SMARCA4 HGNC:11100
509 SWI/SNF related BAF chromatin remodeling complex subunit B1 SMARCB1 HGNC:11103
510 SWI/SNF related BAF chromatin remodeling complex subunit E1 SMARCE1 HGNC:11109
511 Smoothened, frizzled class receptor SMO HGNC:11119
512 Snail family transcriptional repressor 1 SNAI1 HGNC:11128
513 Snail family transcriptional repressor 2 SNAI2 HGNC:11094
514 Small nucleolar RNA host gene 1 SNHG1 HGNC:32688
515 Small nucleolar RNA host gene 12 SNHG12 HGNC:30062
516 Small nucleolar RNA host gene 15 SNHG15 HGNC:27797
517 Small nucleolar RNA host gene 7 SNHG7 HGNC:28254
518 Suppressor of cytokine signaling 1 SOCS1 HGNC:19383
519 Superoxide dismutase 2 SOD2 HGNC:11180
520 SRY-box transcription factor 2 SOX2 HGNC:11195
521 SOX2 overlapping transcript SOX2-OT HGNC:20209
522 SRY-box transcription factor 9 SOX9 HGNC:11204
523 Sp1 transcription factor SP1 HGNC:11205
524 Spen family transcriptional repressor SPEN HGNC:17575
525 Secreted phosphoprotein 1 SPP1 HGNC:11255
526 ST8SIA6 antisense RNA 1 ST8SIA6-AS1 HGNC:44880
527 STAG2 cohesin complex component STAG2 HGNC:11355
528 Signal transducer and activator of transcription 1 STAT1 HGNC:11362
529 Signal transducer and activator of transcription 3 STAT3 HGNC:11364
530 Signal transducer and activator of transcription 5B STAT5B HGNC:11367
531 Steroid sulfatase STS HGNC:11425
532 STXBP5 antisense RNA 1 STXBP5-AS1 HGNC:44183
533 SUFU negative regulator of hedgehog signaling SUFU HGNC:16466
534 T-box transcription factor 3 TBX3 HGNC:11602
535 Transcription factor 7 like 2 TCF7L2 HGNC:11641
536 TEK receptor tyrosine kinase TEK HGNC:11724
537 Telomerase reverse transcriptase TERT HGNC:11730
538 Transforming growth factor alpha TGFA HGNC:11765
539 Transforming growth factor beta 1 TGFB1 HGNC:11766
540 Transforming growth factor beta 2 TGFB2 HGNC:11768
541 Transforming growth factor beta receptor 1 TGFBR1 HGNC:11772
542 Transforming growth factor beta receptor 3 TGFBR3 HGNC:11774
543 Thrombospondin 1 THBS1 HGNC:11785
544 TIMP metallopeptidase inhibitor 1 TIMP1 HGNC:11820
545 TIMP metallopeptidase inhibitor 2 TIMP2 HGNC:11821
546 TIMP metallopeptidase inhibitor 3 TIMP3 HGNC:11822
547 Toll like receptor 4 TLR4 HGNC:11850
548 Transmembrane protein 127 TMEM127 HGNC:26038
549 Tumor necrosis factor TNF HGNC:11892
550 TNF receptor superfamily member 10b TNFRSF10B HGNC:11905
551 TNF superfamily member 10 TNFSF10 HGNC:11925
552 Tankyrase TNKS HGNC:11941
553 DNA topoisomerase I TOP1 HGNC:11986
554 DNA topoisomerase II alpha TOP2A HGNC:11989
555 DNA topoisomerase II beta TOP2B HGNC:11990
556 Tumor protein p53 TP53 HGNC:11998
557 Tumor protein p53 binding protein 1 TP53BP1 HGNC:11999
558 Tumor protein p63 TP63 HGNC:15979
559 Tumor protein p73 TP73 HGNC:12003
560 Trophoblast glycoprotein TPBG HGNC:12004
561 Tropomyosin 1 TPM1 HGNC:12010
562 TNF receptor associated factor 5 TRAF5 HGNC:12035
563 Tripartite motif containing 24 TRIM24 HGNC:11812
564 TSC complex subunit 1 TSC1 HGNC:12362
565 TSC complex subunit 2 TSC2 HGNC:12363
566 Tumor susceptibility 101 TSG101 HGNC:15971
567 Thyroid stimulating hormone receptor TSHR HGNC:12373
568 Tubulin beta class I TUBB HGNC:20778
569 Taurine up-regulated 1 TUG1 HGNC:26066
570 Twist family bHLH transcription factor 1 TWIST1 HGNC:12428
571 Thymidine phosphorylase TYMP HGNC:3148
572 Thymidylate synthetase TYMS HGNC:12441
573 Urothelial cancer associated 1 UCA1 HGNC:37126
574 Ubiquitin interaction motif containing 1 UIMC1 HGNC:30298
575 Vitamin D receptor VDR HGNC:12679
576 Vascular endothelial growth factor A VEGFA HGNC:12680
577 Vascular endothelial growth factor C VEGFC HGNC:12682
578 von Hippel-Lindau tumor suppressor VHL HGNC:12687
579 Vimentin VIM HGNC:12692
580 WEE1 G2 checkpoint kinase WEE1 HGNC:12761
581 Wnt family member 5A WNT5A HGNC:12784
582 WD repeat containing antisense to TP53 WRAP53 HGNC:25522
583 WRN RecQ like helicase WRN HGNC:12791
584 WT1 transcription factor WT1 HGNC:12796
585 WW domain containing oxidoreductase WWOX HGNC:12799
586 X-box binding protein 1 XBP1 HGNC:12801
587 X-linked inhibitor of apoptosis XIAP HGNC:592
588 X inactive specific transcript XIST HGNC:12810
589 XPA, DNA damage recognition and repair factor XPA HGNC:12814
590 XPC complex subunit, DNA damage recognition and repair factor XPC HGNC:12816
591 X-ray repair cross complementing 1 XRCC1 HGNC:12828
592 X-ray repair cross complementing 2 XRCC2 HGNC:12829
593 X-ray repair cross complementing 3 XRCC3 HGNC:12830
594 Yes1 associated transcriptional regulator YAP1 HGNC:16262
595 Zinc finger E-box binding homeobox 1 ZEB1 HGNC:11642
596 Zinc finger E-box binding homeobox 2 ZEB2 HGNC:14881
597 ZNFX1 antisense RNA 1 ZFAS1 HGNC:33101
598 Zinc finger homeobox 3 ZFHX3 HGNC:777
599 Zinc finger protein 226 ZNF226 HGNC:13019
600 Apurinic/apyrimidinic endodeoxyribonuclease 1 APEX1 HGNC:587
Supplementary Table 5: The DC, BC and CC values of the top 23 genes with high node degrees.
S. no. Gene Degree Betweenness Closeness
1 TP53 20 36.55488 0.9166667
2 CTNNB1 17 22.947418 0.8148148
3 STAT3 16 35.14751 0.78571427
4 EP300 15 6.983542 0.7586207
5 BRCA1 15 8.865761 0.7586207
6 JUN 15 6.3675547 0.7586207
7 HDAC1 14 7.10359 0.73333335
8 SMAD3 14 11.143892 0.73333335
9 FOXO3 14 9.667524 0.73333335
10 EGFR 14 30.097809 0.73333335
11 HIF1A 13 4.958153 0.7096774
12 CREBBP 13 3.048002 0.7096774
13 HSP90AA1 13 14.258073 0.7096774
14 CDK2 13 6.858516 0.6875
15 SMAD2 11 5.4929295 0.6666667
16 CDK4 11 5.385622 0.64705884
17 SMARCA4 10 3.1275735 0.62857145
18 ATM 10 4.311977 0.6111111
19 GRB2 7 6.6081953 0.5945946
20 CDKN1B 7 4.7634 0.5945946
21 PTPN11 6 3.5929294 0.5641026
22 CD44 6 0.7151515 0.57894737
23 SHC1 4 0 0.5
Supplementary Table 6: The DC, BC and CC values of the top 15 compounds with node degrees.
S. no. Compound Degree Betweenness Closeness
1 Norcepharadione B 16 0.044930636 0.569231
2 Piperine 10 0.007306859 0.480519
3 Aristolodione 18 0.084677764 0.606557
4 Aristolactam BII 12 0.021652833 0.506849
5 Piperlongumine 11 0.017921943 0.493333
6 Pluviatilol 15 0.034154909 0.55223881
7 Aristololactam 12 0.032323994 0.506849
8 Fargesin 11 0.012610539 0.49333333
9 Pellitorine 20 0.163497384 0.64912281
10 Aristolactam AII 18 0.085932008 0.60655738
11 Piperettine 10 0.007306859 0.48051948
12 Asarinine 11 0.012222268 0.49333333
13 Demethoxypiplartine 10 0.015304632 0.480519
14 N-isobutyl decadienamide 15 0.058820693 0.552239
15 Sesamin 11 0.01244779 0.493333
Supplementary Table 7: List of protein-ligand complexes with top 5 binding affinities.
S. no. Protein-ligand complex Predicted docking scores (kcal/mol)
1 TP53_Norcepharadione B −6.7
2 TP53_Aristolodione −7.1
3 TP53_Pellitorine −5.1
4 TP53_Aristolactam AII −6.6
5 TP53_N-isobutyl decadienamide −5.8
6 CTNNB1_Norcepharadione B −6.4
7 CTNNB1_Aristolodione −6.9
8 CTNNB1_Pellitorine −4.8
9 CTNNB1_Aristolactam AII −6.3
10 CTNNB1_N-isobutyl decadienamide −5.6
11 HSP90AA1_Norcepharadione B −10.9
12 HSP90AA1_Aristolodione −10.3
13 HSP90AA1_Pellitorine −7.5
14 HSP90AA1_Aristolactam AII −10.7
15 HSP90AA1_N-isobutyl decadienamide −9
16 SMAD3_Norcepharadione B −7
17 SMAD3_Aristolodione −6.7
18 SMAD3_Pellitorine −5.2
19 SMAD3_Aristolactam AII −6.6
20 SMAD3_N-isobutyl decadienamide −6.3
21 STAT3_Norcepharadione B −7.2
22 STAT3_Aristolodione −7.6
23 STAT3_Pellitorine −5.5
24 STAT3_Aristolactam AII −6.9
25 STAT3_N-isobutyl decadienamide −6.5
26 EGFR_Norcepharadione B −8.9
27 EGFR_Aristolodione −9.1
28 EGFR_Pellitorine −5.3
29 EGFR_Aristolactam AII −8.4
30 EGFR_N-isobutyl decadienamide −6.4
Supplementary Table 8: MTT analysis data.
Extract concentration Proliferation percentages Mean Standard deviation
Replicate 1 Replicate 2 Replicate 3
Blank 100 100 100 100 0
0.25 μg/mL 96.07 98.87 99.97 98.3033333 2.01080415
0.5 μg/mL 99.29 98.43 94.76 97.4933333 2.40587475
1 μg/mL 98.81 99.06 94.42 97.43 2.60973179
2.5 μg/mL 99.46 98.37 88.76 95.53 5.888268
3.75 μg/mL 47.66 49.17 52.19 49.6733333 2.3065631
5 μg/mL 39.48 41.1 37.89 39.49 1.60502336
7.5 μg/mL 3.71 4.42 5.91 4.68 1.12280898
10 μg/mL 3.35 5.06 10.55 6.32 3.76174162
12.5 μg/mL 3.75 6.44 8.06 6.08333333 2.17702396
15 μg/mL 3.1 3.18 5.73 4.00333333 1.4958721
20 μg/mL 1.04 9.72 2.56 4.44 4.63534249
25 μg/mL 4.03 6.42 1.76 4.07 2.3302575
30 μg/mL 7.94 4.03 2.19 4.72 2.93644343
50 μg/mL 5.89 4.39 3.87 4.71666667 1.04887241