Mimicry of antimicrobial host-defense peptides by random copolymers

被引：394

作者：

Mowery, Brendan P. ^{[1
]}

Lee, Sarah E. ^{[1
]}

Kissounko, Denis A. ^{[1
]}

Epand, Raquel F. ^{[3
]}

Epand, Richard M. ^{[3
]}

Weisblum, Bernard ^{[2
]}

Stahl, Shannon S. ^{[1
]}

Gellman, Samuel H. ^{[1
]}

机构：

[1] Univ Wisconsin, Dept Chem, Madison, WI 53706 USA

[2] Univ Wisconsin, Dept Pharmacol, Madison, WI 53706 USA

[3] McMaster Univ, Hlth Sci Ctr, Dept Biochem & Biomed Sci, Hamilton, ON L8N 3Z5, Canada

来源：

JOURNAL OF THE AMERICAN CHEMICAL SOCIETY | 2007年 / 129卷 / 50期

关键词：

D O I：

10.1021/ja077288d

中图分类号：

O6 [化学];

学科分类号：

0703 ;

摘要：

Efforts to generate antibacterial agents via mimicry of host-defense peptides have focused on discrete oligomers that can adopt a regular globally amphiphilic conformation in the presence of bacterial cell membranes and ultimately disrupt those membranes. Although considerable success has been achieved with this approach, application of the resulting molecules is hampered by the high cost associated with stepwise oligomer synthesis. We show that random poly-beta-peptide copolymers, prepared by ring-opening polymerization of beta-lactams, can be tuned to display good activity against a panel of four bacteria along with low lytic activity toward human red blood cells. These findings support a nonclassical design hypothesis for antibacterial agents.

引用

页码：15474 / +

页数：4

共 38 条

[1] A right handed peptide helix containing a central double D-amino acid segment [J].