Enhancing membrane disruption by targeting and multivalent presentation of antimicrobial peptides

被引：33

作者：

Chamorro, Cristina ^{[1
,2
]}

Boerman, Marcel A. ^{[1
]}

Arnusch, Christopher J. ^{[1
,2
]}

Breukink, Eefjan ^{[2
]}

Pieters, Roland J. ^{[1
]}

机构：

[1] Univ Utrecht, Inst Pharmaceut Sci, Dept Med Chem & Chem Biol, NL-3508 TB Utrecht, Netherlands

[2] Univ Utrecht, Inst Biomembranes, Dept Biochem Membranes, Bijvoet Ctr, NL-3508 TB Utrecht, Netherlands

来源：

BIOCHIMICA ET BIOPHYSICA ACTA-BIOMEMBRANES | 2012年 / 1818卷 / 09期

关键词：

Antimicrobial peptide; Targeting; Multivalency; Membrane disruption; Anoplin; Temporin L; LIPID-II; MECHANISM; DESIGN; ANTIBIOTICS; SELECTIVITY; ANOPLIN;

D O I：

10.1016/j.bbamem.2012.04.004

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

In order to enhance the membrane disruption of antimicrobial peptides both targeting and multivalent presentation approaches were explored. The antimicrobial peptides anoplin and temporin L were conjugated via click chemistry to vancomycin and to di- and tetravalent dendrimers. The vancomycin unit led to enhanced membrane disruption of large unilamellar vesicles (LUVs) displaying the vancomycin target lipid II, but only for temporin L and not for anoplin. The multivalent presentation led to enhanced LUV membrane disruption in the case of anoplin but not for temporin L. (C) 2012 Elsevier B.V. All rights reserved.

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收藏

页码：2171 / 2174

页数：4

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