EXPLORING THE ROLE OF C–H … π INTERACTIONS ON THE STRUCTURAL STABILITY OF ANTIMICROBIAL PEPTIDES

Abstract

A computational analysis on the C – H … π interactions in a group of 53 antimicrobial peptides was investigated. A total of 162 C – H … π interactions were observed. Side-chain to side-chain C – H … π interactions are the predominant type of interactions in antimicrobial peptides data set. There was an average of one significant C – H … π interaction for every 7 residues in the antimicrobial peptides investigated. Long-range C – H … π interactions are the predominant type of interactions. The secondary structure preference, solvent accessibility and stabilization centers of these of C – H … π interacting residues were estimated. It is likely that the C – H … π interactions contribute significantly to the overall stability of antimicrobial peptides. These interactions were observed after a molecular dynamics study on these set of antimicrobial peptides using CHARMM force field.