3D peptide-protein docking between a novel peptide derived from Boerhavia diffusa and a Cervical cancer protein, Transmembrane Protein 50A (TM50A), using insilico strategies

Abstract

The current study's goal is to identify a potential peptide-based drug to treat cervical cancer in humans. The matK gene-coded protein sequence, Maturase K was isolated from the plant, Boerhavia diffusa, in order to identify a new peptide targeting cervical cancer protein target, TM50A (Transmembrane protein 50A). An Immunomedicine technique was used to identify the relevant antigenic binding sites in the amino acid sequence. The Swiss Model Server was used to predict the anticipated antigenic peptide sequence. The peptide was modelled using techniques such as ProQ3, IDDT, and QMEANDisCo. The sequence alignment makes it abundantly evident that our sequence structure is devoid of both sequence similarity and prior deposition. The newly identified peptide sequence (SFQALLERIYFHVKIEYLVKVLTKNCRIILWLFKDPFTHYIRYQGKSILS) was 50 aa long. Drug docking tests were used to identify the medications that might bind to the identified peptide structure. The cancer protein may be down-regulated during drug binding interactions if certain regions exhibit intermolecular H-bond interactions. We developed a simulation of the structure to aid researchers working on structure-based drug design studies. To help researchers in the field of cancer informatics, our structure has been deposited in PDB-IHM -ModelArchive (https://modelarchive.org/DOI/10.5452/ma-4whza/).