The impact of charged particles on beta-glucosidase and its molecular dynamics mechanism: A deep insight into the effects of charged peptides on enzyme activity and conformation

Abstract

Beta-Glucosidase(BGL) is an enzyme present in all organisms and plays a key role in a variety of biological processes. In this study, three short peptides Z1, O1, and F1 with positive, neutral, and negative charges, respectively, were designed and synthesised, which were added to the BGL system of action, and the changes in BGL activity and conformation induced by the charged short peptides were investigated by measuring changes in enzyme activities and zeta potentials, as well as by applying spectroscopy and computer simulation. The results showed that Z1 increased BGL activity and zeta potential by 54.6 %, on the contrary, the negatively charged short peptide F1 inhibited its enzyme activity and decreased the potential by 38.3 %, and O1 had less effect on BGL. The results of spectroscopy and computer simulation showed that the addition of the charged short peptide led to significant changes in the apparent morphology and structure of BGL, but it did not bind to BGL to form a complex, but rather affected its surface charge distribution and altered the enzymatic activity and structure of BGL.