Banca de DEFESA: Amanda Maria de Souza Nascimento

Uma banca de DEFESA de MESTRADO foi cadastrada pelo programa.
STUDENT : Amanda Maria de Souza Nascimento
DATE: 30/08/2021
TIME: 08:30
LOCAL: Sessão pública realizada por meio de vídeo conferência
TITLE:

Antibacterial action mechanisms of trypsin inhibitors: a systematic review and in silico study of molecular dynamics simulation with bacterial membranes

KEY WORDS:

Antibacterial peptide, bacterial culture, computational simulation

PAGES: 84
BIG AREA: Ciências da Saúde
AREA: Nutrição
SUMMARY:

The knowledge of new antimicrobial compounds capable of acting against microorganisms deserves special attention today. Several molecules of plant origin have been studied for their antibacterial activities, and among them are trypsin inhibitors, especially the purified trypsin inhibitor from tamarind seeds (TTIp). The present work aimed to present the antibacterial action mechanisms of trypsin inhibitors through a systematic review (SR) and an in silico study of molecular dynamics simulation (MDS). Similar studies published in the literature were gathered for the review to answer the following question: What are the antibacterial action mechanisms of trypsin inhibitor peptides and proteins? Initially, a SR protocol was designed and registered in the prospective international registry of systematic reviews (PROSPERO). Thus, the Preferred Reporting Items Checklist for Systematic Review and Meta-Analysis Protocols (PRISMA-P) was used to delineate the protocol and PRISMA for the systematic review. The articles were selected according to eligibility criteria according to PICOS (population, interventions, control, results, and study type). The databases used for the research were PubMed, ScienceDirect, Scopus, Web of Science, BVS, and EMBASE. Original articles resulting from studies with rats and/or mice, in vitro studies (bacterial culture), and with cells cultures were included, which described the treatments, effects and antibacterial mechanisms of peptides or proteins of the trypsin inhibitor type. Articles were selected, and two independent reviewers extracted data. The assessment of the methodological quality of each survey was performed using the OHAT (Office of Health Assessment and Translation) tool. The review protocol was registered in PROSPERO under number: CRD42020189069. In the SR, 2382 articles were retrieved, with 17 eligible for review at the end of the search. Only three studies have gone into the effect directly on the bacterial cytoplasmic membrane, two against S. aureus, Gram-positive bacteria (GP), both causing membrane disturbance. In a third study, the antibacterial effect was attributed to inhibition of endogenous proteases extracted from the bacteria themselves (S. enterica and S. aureus). For the MDS simulation study, model number 56 was used in conformation number 287 of the TTIp (TTIp 56/287), and the lipid bilayer model generated by the CHARMM-GUI server to evaluate the structural behavior and interactions by MDS simulations were performed using the Gromacs package 5.1.2. A greater interaction of TTIp 56/287 with the GP membrane was observed, presenting potential energy of interaction (PEI) of –1094.97 kcal.mol1, when compared to the interaction with the Gram-negative membrane (GN) of -444,337 kcal.mol1. It was possible to identify that in the interaction TTIp 56/287-GP, the amino acid residues of arginine showed higher PEI, while in the interaction TTIp 56/287-GN, they were with the residues of glutamine. Thus, this study firstly clarifies and systematizes the antibacterial action of these trypsin inhibitor-type proteins, being of great relevance and generating information for possible future research on these pathways. Additionally, the MDS simulation study points out the TTIp as a candidate for future studies that consolidate it as an option in the most effective treatment of bacterial infections.

BANKING MEMBERS:
Externa à Instituição - RAQUEL DE OLIVEIRA ROCHA
Presidente - 2578619 - ANA HELONEIDA DE ARAUJO MORAIS
Externa ao Programa - 2665457 - GIDYENNE CHRISTINE BANDEIRA SILVA DE MEDEIROS
Interna - 3211846 - KARLA SUZANNE FLORENTINO DA SILVA CHAVES DAMASCENO