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

被引：8
|
作者：
Bagheri, Mojtaba [1 ]
机构：
[1] Univ Tehran, Dept Biochem, Inst Biochem & Biophys, Tehran 1417614411, Iran
来源：
CHEMISTRYOPEN | 2015年 / 4卷 / 03期
关键词：
antimicrobial peptides; immobilization; liposomes; materials; thermodynamics;
D O I：
10.1002/open.201402149
中图分类号：
O6 [化学];
学科分类号：
0703 ;
摘要：
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. © 2014 The Authors. Published by Wiley-VCH Verlag GmbH & Co. KGaA.
引用
收藏
页码：389 / 393
页数：5
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