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beta-Sheet-breaking peptides inhibit the fibrillation of human alpha-synuclein.

作者信息

Kim You Soon, Lim Dongyeol, Kim Joo Yeon, Kang Shin Jung, Kim Yang-Hee, Im Hana

机构信息

Department of Molecular Biology, Sejong University, Seoul, Republic of Korea.

出版信息

Biochem Biophys Res Commun. 2009 Oct 2;387(4):682-7. doi: 10.1016/j.bbrc.2009.07.083. Epub 2009 Jul 19.

DOI:10.1016/j.bbrc.2009.07.083
PMID:19622344
Abstract

alpha-Synuclein is the major components of the intracellular protein-aggregates, found in the dopaminergic neurons of Parkinson's disease patients. Previously, we screened for alpha-synuclein substitution mutants that prevent fibril formation of both wild-type and Parkinson's disease-linked alpha-synuclein variants. In the present study, we show that short synthetic peptides derived from these mutant sequences not only prevented alpha-synuclein fibrillation but also dissolved preformed alpha-synuclein aggregates in vitro. The hexapeptide PGVTAV, which was the shortest peptide that retained the ability to block alpha-synuclein fibrillation, may serve as a lead compound for the development of therapeutics for Parkinson's disease.

摘要

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