Influence of Salt on the Self-Assembly of Two Model Amyloid Heptapeptides

被引：51

作者：

Castelletto, V. ^{[1
]}

Hamley, I. W. ^{[1
,3
]}

Cenker, C. ^{[2
]}

Olsson, U. ^{[2
]}

机构：

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

[2] Lund Univ, S-22100 Lund, Sweden

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

来源：

JOURNAL OF PHYSICAL CHEMISTRY B | 2010年 / 114卷 / 23期

基金：

英国工程与自然科学研究理事会;

关键词：

BETA-PEPTIDES; CONFORMATION; SPECTROSCOPY; DEPENDENCE; INHIBITORS; MORPHOLOGY; STABILITY; NANOTUBES; RESIDUE; NMR;

D O I：

10.1021/jp102744g

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：

We study the effects of NaCl on the self-assembly of AAKLVFF and beta A beta AKLVFF in solution. Both AAKLVFF and beta A beta AKLVFF self-assemble into twisted fibers in aqueous solution. The addition of NaCl to aqueous solutions of AAKLVFF produces large crystal-like nanotapes which eventually precipitate. In contrast, highly twisted fibrils were observed for beta A beta AKLVFF solutions at low salt concentration, while a coexistence of highly twisted fibers and nanotubes was observed for beta A beta AKLVFF at high salt concentration. The self-assembled structures observed for beta A beta AKLVFF in NaCl solutions were ascribed to the progressive screening of the beta A beta AKLVFF surface charge caused by the addition of salt.

引用

页码：8002 / 8008

页数：7

共 38 条

[1] Exploring the antibacterial and hemolytic activity of shorter- and longer-chain β- α,β-, and γ-peptides, and of β-peptides from β2-3-aza- and β3-2-methylidene-amino acids bearing proteinogenic side chains -: A survey [J].