Reversible helical unwinding transition of a self-assembling peptide amphiphile

被引：73
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
收藏
页码：9290 / 9293
页数：4
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