Cationic Antimicrobial Peptides (AMPs): Thermodynamic Characterization of Peptide-Lipid Interactions and Biological Efficacy of Surface-Tethered Peptides

Abstract

Antimicrobial peptides (AMPs) were investigated both as novel antibiotics and as antimicrobial coatings for biomedical implants. The hydrophobicity, conformational constraint, and strong binding of cyclo-RRRWFW (c-WFW) to the O-antigen region of lipopolysaccharide (LPS) were identified as important features for potent anti-E. coli activity. Furthermore, tethered membrane-active AMPs with uniform distribution of cationic and hydrophobic amino acid residue were identified as good anti-biofilm agents.