Role of the Conformational Rigidity in the Design of Biomimetic Antimicrobial Compounds

被引：51
|
作者：
Ivankin, Andrey [1 ,2 ]
Livne, Liran [3 ]
Mor, Amram [3 ]
Caputo, Gregory A. [4 ]
DeGrado, William F. [5 ]
Meron, Mati [6 ]
Lin, Binhua [6 ]
Gidalevitz, David [1 ,2 ]
机构：
[1] IIT, Ctr Mol Study Condensed Soft Matter uCoSM, Chicago, IL 60616 USA
[2] IIT, Div Phys, BCPS Dept, Chicago, IL 60616 USA
[3] Technion Israel Inst Technol, Dept Biotechnol & Food Engn, IL-32000 Haifa, Israel
[4] Rowan Univ, Dept Chem & Biochem, Glassboro, NJ 08028 USA
[5] Univ Penn, Sch Med, Dept Biochem & Biophys, Philadelphia, PA 19104 USA
[6] Univ Chicago, CARS, Chicago, IL 60637 USA
来源：
ANGEWANDTE CHEMIE-INTERNATIONAL EDITION | 2010年 / 49卷 / 45期
基金：
以色列科学基金会; 美国国家科学基金会;
关键词：
antimicrobial peptides; chemical mimicry; conformational analysis; membranes; mode of interaction; HOST-DEFENSE PEPTIDES; LL-37; PROTEGRIN;
D O I：
10.1002/anie.201003104
中图分类号：
O6 [化学];
学科分类号：
0703 ;
摘要：
When structural flexibility is a plus: A link between structural flexibility of biomimetic antimicrobials and their ability to penetrate into the hydrophobic core and disrupt the integrity of bacterial lipid model membranes has been established using liquid surface X-ray scattering techniques. Results indicate that the modes of interaction of flexible and conformationally restrained antimicrobials with the bacterial membranes are different (see picture). © 2010 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim.
引用
收藏
页码：8462 / 8465
页数：4
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