Direct Observation of Time-Resolved Polymorphic States in the Self-Assembly of End-Capped Heptapeptides

被引：110

作者：

Adamcik, Jozef ^{[2
]}

Castelletto, Valeria ^{[1
]}

Bolisetty, Sreenath ^{[2
]}

Hamley, Ian W. ^{[1
]}

Mezzenga, Raffaele ^{[2
]}

机构：

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

[2] Swiss Fed Inst Technol, Inst Food Nutr & Hlth, CH-8092 Zurich, Switzerland

来源：

ANGEWANDTE CHEMIE-INTERNATIONAL EDITION | 2011年 / 50卷 / 24期

基金：

英国工程与自然科学研究理事会;

关键词：

atomic force microscopy; helical structures; nanotubes; peptides; single-molecule studies; BETA-AMYLOID FIBRILS; PEPTIDE NANOTUBES; PROTEIN; MODEL; RIBBONS; MOLECULES; FRAGMENT;

D O I：

10.1002/anie.201100807

中图分类号：

O6 [化学];

学科分类号：

0703 ;

摘要：

Fibrillation processes in peptides: Structural states in the time-dependent self-assembly of an amyloid heptapeptide were resolved by single-molecule atomic force microscopy. Statistical analysis of the structures and their topological details revealed a continuous evolution of the polymorphs over time from the initial small spherical micelles into protofilaments, helical ribbons, and finally nanotube-like structures (see picture). Copyright © 2011 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim.

引用

页码：5495 / 5498

页数：4

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