Huntingtin aggregation monitored by dynamic light scattering

被引：56

作者：

Georgalis, Y

Starikov, EB

Hollenbach, B

Lurz, R

Scherzinger, E

Saenger, W

Lehrach, H

Wanker, EE

机构：

[1] Max Planck Inst Mol Genet, D-14195 Berlin, Germany

[2] Free Univ Berlin, Inst Kristallog, D-14195 Berlin, Germany

来源：

PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA | 1998年 / 95卷 / 11期

关键词：

Huntington's disease; fibrillogenesis;

D O I：

10.1073/pnas.95.11.6118

中图分类号：

O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];

学科分类号：

07 ; 0710 ; 09 ;

摘要：

An initial stage of fibrillogenesis in solutions of glutathione S-transferase-huntingtin (GST-HD) fusion proteins has been studied by using dynamic light scattering. Two GST-HD systems with poly-L-glutamine (polyGln) extensions of different lengths (20 and 51 residues) have been examined. For both systems, kinetics of z-average translation diffusion coefficients (D-app) and their angular dependence have been obtained. Our data reveal that aggregation does occur in both GST-HD51 and GST-HD20 solutions, but that it is much more pronounced in the former. Thus, our approach provides a powerful tool for the quantitative assay of GST-HD fibrillogenesis in vitro.

引用

页码：6118 / 6121

页数：4

共 28 条

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