Huntingtin aggregation monitored by dynamic light scattering

Item Type:	Article
Title:	Huntingtin aggregation monitored by dynamic light scattering
Creators Name:	Georgalis, Y. and Starikov, E.B. and Hollenbach, B. and Lurz, R. and Scherzinger, E. and Saenger, W. and Lehrach, H. and Wanker, E.E.
Abstract:	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 (Dapp) 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.
Keywords:	Huntington’s Disease, Fibrillogenesis
Source:	Proceedings of the National Academy of Sciences of the United States of America
ISSN:	0027-8424
Publisher:	National Academy of Sciences
Volume:	95
Number:	11
Page Range:	6118-6121
Date:	26 May 1998
Official Publication:	https://doi.org/10.1073/pnas.95.11.6118
PubMed:	View item in PubMed

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