Reversible helical unwinding transition of a self-assembling peptide amphiphile

被引：75

作者：

Hamley, Ian W. ^{[1
]}

Dehsorkhi, Ashkan ^{[1
]}

Castelletto, Valeria ^{[1
]}

Furzeland, Steve ^{[2
]}

Atkins, Derek ^{[2
]}

Seitsonen, Jani ^{[3
]}

Ruokolainen, Janne ^{[3
]}

机构：

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

[2] Colworth Discover Unilever R&D, Sharnbrook MK44 1LQ, Beds, England

[3] Aalto Univ, Sch Sci, Dept Appl Phys, FI-00076 Aalto, Finland

来源：

SOFT MATTER | 2013年 / 9卷 / 39期

基金：

英国工程与自然科学研究理事会;

关键词：

AMYLOID-BETA-PEPTIDE; THIOFLAVIN-T; INFRARED-SPECTROSCOPY; RIBBONS; PROTEINS; TUBULES; FIBRILLIZATION; ALZHEIMERS; FRAGMENT; FIBRILS;

D O I：

10.1039/c3sm51725j

中图分类号：

O64 [物理化学（理论化学）、化学物理学];

学科分类号：

070304 ; 081704 ;

摘要：

A designed peptide amphiphile C-16-KKFFVLK self-assembles into nanotubes and helical ribbons in aqueous solution at room temperature. A remarkable unwinding transition, leading to twisted tapes, is observed on heating. Nanotubes and ribbons re-form on cooling.

引用

页码：9290 / 9293

页数：4

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