Enhancing bioactivity of pediocin-like bacteriocins through molecular and structural in silico approaches

Abstract

Bacteriocins are antimicrobial peptides naturally produced by some lactic acid bacteria, highlighted for their inhibitory activities, particularly against some foodborne pathogens such as Listeria, for which pediocin-like bacteriocins stand out as antimicrobial agents. However, there is still much improvement to be made for the optimization of this strategy to replace antibiotics. The analysis of sequence and structure of bacteriocins through in silico methods allows the identification of peptides and respective molecular targets for simulation of interactions, aiming to improve their bioactivities. The present study includes the comparative analysis of multiple sequences of pediocin-like bacteriocins, their respective molecular modelling, mechanics and dynamics, identification of molecular targets and proposals for structural modifications. For that, three-dimensional models will be built, binding energies calculated and molecular dynamics simulated. We aim to obtain information regarding diversity of sequences, functional motifs, identification of targets, conformational states and phylogeny of bacteriocins and producer bacteria, in order to propose structural modification for the enhancement of antimicrobial activity. Thus, these studied peptides can help to save resources and provide better efficiency on combating relevant pathogens for the food industry and public health. It represents a notable step in finding probiotic applications, aiming to improve food quality and global health.