مشخصات پژوهش

The most membrane peptide use as antibacterials produced by one species of microbe (Bacillus brevis). developing the antimicrobial peptides are recently focused on Pharmacists , since they serve as antibacterials in prevailing over drug resistance by eliciting the disruption of microbial membrane. Still, there are lots of challenges to bring up the structurally stable and functionally efcient antimicrobial peptides. This study analyzes the structural stability and the functional activity of gramicidin-C peptide in lipid bilayers membrane, thereby demonstrating its potent antibacterial activity against antibiotic-resistant micro-organisms. To investigate the structural stability and functionality of gramicidin C, we performed dynamic analysis VMD-1.9.3 package . The structure and lateral pressure profile of the 1,2- dimyristoyl-sn-glycero-3-phosphatidylcholine (DMPC) lipid bilayers in the absence and presence of gramicidin C (GC) are studied by molecular dynamics simulation. In the absence of detailed structural and biophysical/biochemical characterization of protein/lipid interactions, Molecular dynamics (MD) simulations are able to provide a key tool, for probing the interactions of lipids with membrane proteins. In conclusion, gramicidin-C peptide has defnitely demonstrated adequate structural stability and functionality and this work will need to be considered in peptide-based drug discovery.