The position of hydrophobic residues tunes peptide self-assembly

被引：13

作者：

Bortolini, Christian ^{[1
,2
]}

Liu, Lei ^{[1
,3
]}

Gronewold, Thomas M. A. ^{[4
]}

Wang, Chen ^{[2
]}

Besenbacher, Flemming ^{[1
]}

Dong, Mingdong ^{[1
]}

机构：

[1] Interdisciplinary Nanosci Ctr iNANO, Aarhus C, Denmark

[2] Natl Ctr Nanosci & Technol NCNST, Beijing, Peoples R China

[3] JiangSu Univ, Inst Adv Mat, Zhenjiang, Peoples R China

[4] SAW Instruments GmbH Schwertberger, D-53177 Bonn, Germany

来源：

SOFT MATTER | 2014年 / 10卷 / 31期

基金：

新加坡国家研究基金会;

关键词：

AMYLOID FIBRILS; CYTOTOXICITY; FIBRILLATION; POLYMORPHISM; FRAGMENTS;

D O I：

10.1039/c4sm01065e

中图分类号：

O64 [物理化学（理论化学）、化学物理学];

学科分类号：

070305 [高分子化学与物理];

摘要：

The final structure and properties of synthetic peptides mainly depend on their sequence composition and experimental conditions. This work demonstrates that a variation in the positions of hydrophobic residues within a peptide sequence can tune the self-assembly. Techniques employed are atomic force microscopy, transmission electron microscopy and an innovative method based on surface acoustic waves. In addition, a systematic investigation on pH dependence was carried out by utilizing constant experimental parameters.

引用

页码：5656 / 5661

页数：6

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