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Abstract

Cancer is characterized by dysregulated metabolic signaling pathways, leading to uncontrolled cellular proliferation. Current cancer treatments, which involve surgery, radiotherapy, and chemotherapy, still cause adverse systemic toxicities. Accordingly, one possible effort that can be undertaken is to explore safe anticancer substances from protein sources such as peptides. Bioactive peptides can be isolated by hydrolyzing cowpea (Vigna unguiculata L. Walp) protein with trypsin. The objectives of this study were to isolate and fractionate bioactive peptides from cowpea, to determine the anticancer activity of peptide fractions, to identify active peptide fractions as anticancer agents using Liquid Chromatography High Resolution Mass Spectrometry (LC-HRMS), and to determine the molecular docking results of anticancer peptides with the Epidermal Growth Factor Receptor (EGFR) employing the High Ambiguity Driven Protein-Protein Docking (HADDOCK) method. This study was initiated with defatting and protein separation, proceeded with ammonium sulfate fractionation, dialysis, hydrolysis, and determination of the degree of hydrolysis, fractionation with SPE-PEP, and followed by cytotoxicity testing with BSLT and Resazurin Assay. Identification of the fraction with the highest activity was performed through LC-HRMS, and peptide molecule docking analysis with the EGFR receptor. In the current research, the degree of hydrolysis obtained was 54.3%. The peptide fraction C exhibited the strongest potential anticancer activity, with an IC50 value of 4.19 µg/mL. Identification of the peptide fraction C yielded 12 peptide sequences. P8 and P11 demonstrated peptide interaction with the EGFR receptor, exhibiting the lowest binding affinity of -13.3 kcal/mol, indicating greater stability compared to the other interactions.

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Creative Commons License
This work is licensed under a Creative Commons Attribution-Noncommercial-No Derivative Works 4.0 License.

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