Peptides Organized as Bilayer Membranes

被引：58

作者：

Childers, W. Seth ^{[1
]}

Mehta, Anil K. ^{[1
]}

Ni, Rong ^{[1
]}

Taylor, Jeannette V. ^{[1
]}

Lynn, David G. ^{[1
]}

机构：

[1] Emory Univ, Dept Biol & Chem, Atlanta, GA 30332 USA

来源：

ANGEWANDTE CHEMIE-INTERNATIONAL EDITION | 2010年 / 49卷 / 24期

关键词：

nanomaterials; NMR spectroscopy; peptides; self-assembly; DOUBLE-RESONANCE NMR; SURFACTANT-LIKE PEPTIDES; BETA-AMYLOID PEPTIDE; ANGLE-SPINNING NMR; SOLID-STATE NMR; FORM NANOTUBES; PHOTOSYSTEM-I; EXTENDED TIME; FRAGMENT; SPECTROSCOPY;

D O I：

10.1002/anie.201000212

中图分类号：

O6 [化学];

学科分类号：

0703 ;

摘要：

(Figure Presented) A buried polar bilayer interface composed of interdigitated peptide ends and a high density of CF3COO- counterions passifying lysine amines are identified in nanotubes obtained by self-assembly of short peptides. The structure reveals distinct characteristics that differentiate peptide bilayers and lipid bilayers that can now be exploited for the construction of lipid-like nanomaterials with protein functionality. © 2010 Wiley-VCH Verlag GmbH & Co. KGaA.

引用

页码：4104 / 4107

页数：4

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