In Silico Analysis of Penicillin- Binding Protein 5 As an Inhibitory Target of Beta-Lactam Antibiotics in Enterococcus Faecalis



Yazdi MMK² ; Bahador A¹ Show Affiliations
Source: Der Pharma Chemica Published:2015

Abstract

Enterococcus faecalis is an important pathogen that is associated with a range of infections. Beta-lactam antibiotics are a broad class of antibiotics that are used for treatment of E. faecalis infections, but it has intrinsic and acquired resistance to some of them. Penicillin binding protein (PBP) 5 is one of the members of PBPs family that plays as inhibitors of beta-lactam antibiotics. In this study, we used an in silico strategy and focused on PBP5 in E. faecalis and explained its characterization with the help of bioinformatics tools. The results of primary structure prediction showed that PBP5 is a stable protein and belong to hydrolase protein family. The secondary structure was predicted that random coil is predominantly present followed by extended strand and alpha helix. The three-dimensional structure was modeled using Swiss model workspace and the structure was validated that gives valuable understanding for the improvement of helpful rational strategies for experiments. Ramachandran plot analysis showed that 98% and > 99.8% of all residues of PBP5 were found in favored and allowed regions, respectively. Computer simulation studies, including molecular modeling, having knowledge of PBP5 structure and combination of this information may affect the development of new ways of inhibiting PBP5 to can be designed improved drugs.