Insilico Study and Analysis Antibacterial Activity of Beta-glucan against Beta-Lactamase and Protein Binding Penicillin-2A

Abstract

Beta-lactamase is an enzyme protein that plays a role in the occurrence of antibiotic resistance against Methicillin-resistant Staphylococcus aureus (MRSA) bacteria. This study aims to investigate interactions that occur beta-glucan with Beta-lactamase enzymes and Protein Binding Penicillin-2a (PBP-2a). In this study, the bioinformatics approach or in-silico method was conducted to determine the molecular interactions that occurred computationally. The protein used was Beta-lactamase protein (4ooy), and Protein Binding Penicillin-2a (6h50) obtained from the Protein Data Bank. Beta-glucan as ligand obtained from the PubChem web server. Protein stabilization was carried out to adjust to the body's physiology, carried out using Pymol by removing water atoms and adding hydrogen atoms. Pharma expert web server and Pyrex were used to modulate the interaction between ligand and enzyme. We were analyzed molecular interactions visualization on the molecular complexes generated by docking simulations using the Discovery Studio software. The results showed that beta-glucan has high activity as an antibiotic against Beta-lactamase and PBP-2a. The binding affinity interaction that occurs between Beta-glucan and Beta-lactamase complex interaction was -11.1 kcal/mol, while Beta-glucan and BPP-2a was -8.5 kcal/mol. The interaction bond Beta-glucan and Beta-lactamase was higher than 2s, 5r) -1-Formyl-5 - [(Sulfooxy) amino] piperidine-2-Carboxamid as control ligand. Beta-glucan was predicted to have strong antibacterial properties. However, exploration of beta-glucan compounds and further research to determine the antibacterial effect of beta-glucan against MRSA bacteria.