Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
1933183 | Biochemical and Biophysical Research Communications | 2009 | 6 Pages |
Abstract
α-Synuclein is the major components of the intracellular protein-aggregates, found in the dopaminergic neurons of Parkinson’s disease patients. Previously, we screened for α-synuclein substitution mutants that prevent fibril formation of both wild-type and Parkinson’s disease-linked α-synuclein variants. In the present study, we show that short synthetic peptides derived from these mutant sequences not only prevented α-synuclein fibrillation but also dissolved preformed α-synuclein aggregates in vitro. The hexapeptide PGVTAV, which was the shortest peptide that retained the ability to block α-synuclein fibrillation, may serve as a lead compound for the development of therapeutics for Parkinson’s disease.
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Authors
You Soon Kim, Dongyeol Lim, Joo Yeon Kim, Shin Jung Kang, Yang-Hee Kim, Hana Im,