In silico bioprospecting of receptors for Oligoventin: An antimicrobial peptide isolated from spider eggs of Phoneutria nigriventer

Irresponsible and wholesale use of antimicrobial agents is the principal cause of the emergence of strains of resistant microorganisms to traditional drugs. Oligoventin is a neutral peptide isolated from spider eggs of Phoneutria nigriventer, with antimicrobial activity against Gram-positive, Gram-negative, and yeast organisms. However, the molecular target and pathways of antimicrobial activity are still unknown. Thus, the aim of the present study is to prospect receptors associated with the antimicrobial activity of Oligoventin using in silico tools. The PharmMapper and PDB server was used to prospect targets originating from microorganisms. Additionally, the PatchDock server was utilized to perform molecular docking between Oligoventin and the targets. Subsequently, the I-TASSER server was adopted to predict the ligand site. Finally, the docking results and predicted sites were compared with literature sites of each target. Over 100 potential receptors for oligoventin have been identified. Among these, enoyl-ACP reductase (Idpdb1LXC) and thymidylate synthase ThyX (Idpdb 1O28) from bacteria and N-acetylglucosamine phosphate mutase (Idpdb 2DKD) showed superior interaction with oligoventin, exhibiting colocalization between docked residues and cofactor/active sites. These enzymes play a crucial role in fatty acid and DNA biosynthesis in prokaryotes and in cell wall synthesis in yeast. Therefore, in silico results suggest that Oligoventin can impair fatty acid DNA, cell wall synthesis, thereby reducing microbial proliferation and causing microorganism death. •A total of over 100 potential receptors from microorganisms for Oligoventin have been identified.•Targets with the IDs 1O28, 1M5W, 1TDJ, 1LXC, 1UKQ, and 1KSS exhibited significant docking scores.•Oligoventin interacted with the FAD+ cofactor site of Enoyl-ACP reductase.•Oligoventin interacted with the NAD+ cofactor site of Thymidylate synthase ThyX.•Oligoventin interacted with active site of N-acetylglucosamine-phosphate mutase.