Helical-Ribbon Formation by a β-Amino Acid Modified Amyloid β-Peptide Fragment

被引：81

作者：

Castelletto, Valeria ^{[1
]}

Hamley, Ian W. ^{[1
,2
]}

Hule, Rohan A. ^{[3
,4
]}

Pochan, Darrin ^{[3
,4
]}

机构：

[1] Univ Reading, Dept Chem, Reading RG6 6AD, Berks, England

[2] Diamond Light Source, Didcot OX11 0DE, Oxon, England

[3] Dept Mat Sci, Newark, DE 19716 USA

[4] Delaware Biotechnol Inst, Newark, DE 19716 USA

来源：

ANGEWANDTE CHEMIE-INTERNATIONAL EDITION | 2009年 / 48卷 / 13期

基金：

英国工程与自然科学研究理事会;

关键词：

beta sheets; amyloid beta-peptides; fibrils; helical structures; self-assembly; SYNCHROTRON X-RAY; SECONDARY STRUCTURES; STABILITY; FIBRILS; INHIBITORS; SCATTERING; CORE;

D O I：

10.1002/anie.200805500

中图分类号：

O6 [化学];

学科分类号：

0703 ;

摘要：

An addition to the family: The introduction of β-amino acid residues into a modified amyloid β peptide fragment resulted in well-defined helical nanoribbons (see cryo-TEM image) comprising β strands mainly oriented perpendicular to the ribbon axis. The nanoribbons order into a flowaligning nematic phase at higher concentration. The β-strand nanoribbon structure is an addition to the known set of secondary structures adopted by β-peptides. © 2009 Wiley-VCH Verlag GmbH & Co. KGaA.

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页码：2317 / 2320

页数：4

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