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Abstract
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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.
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