Theoretical study of CHYMO32 peptide obtained by in silico fragmentation of the escapin protein isolated from marine hare Aplysia californica: A prediction for antimicrobial activity

Abstract

AbstractThe scenario involving the alarming growth of bacterial resistance has never been more worrying. Increasingly selective and sophisticated bacterial strains resistant to traditional antibiotics are a threat to the health system worldwide. Therefore, antimicrobial peptides (AMPs) represent a promising path in the fight against multidrug‐resistant pathogens. Here, using an in silico methodology, employing robust software, the present study aims to analyze the chymo32 peptide, obtained by enzymatic fragmentation of the escapin protein to test its possible antibacterial effects, correlating them with their physical–chemical nature. In this study, we used in silico predictions such as structural prediction, physicochemical properties, hemolytic activity, and prediction of activity for immunomodulation. Among the 378 peptide fragments obtained from the original protein, chymo32 was the only peptide selected in the field of screenings involving sequence length, cationicity, hydrophobicity, and prediction of antibacterial activity. The physical–chemical properties of chymo32 are promising, as well as its prediction as AMP. The immunomodulation predictions showed no immunogenic potential, which indicates greater safety in the posterior steps in vitro, also highlighting the absence of hemolytic activity, one of the main problems associated with AMPs in the therapeutic clinic.