Open AccessCationic Antimicrobial Peptides (AMPs): Thermodynamic Characterization of Peptide–Lipid Interactions and Biological Efficacy of Surface‐Tethered Peptides
Author(s) -
Bagheri Mojtaba
Publication year - 2015
Publication title -
chemistryopen
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.644
H-Index - 29
ISSN - 2191-1363
DOI - 10.1002/open.201402149
Subject(s) - antimicrobial peptides , antimicrobial , antibiotics , peptide , cathelicidin , chemistry , escherichia coli , biofilm , microbiology and biotechnology , biochemistry , bacteria , biology , genetics , gene
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.