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The hexapeptide PGVTAV suppresses neurotoxicity of human ?-synuclein aggregates.
Biochem Biophys Res Commun. 2011 May 6;408(2):334-8
Authors: Choi MY, Kim YS, Lim D, Kang SJ, Kim YH, Lee K, Im H
Abstract
In Parkinson's disease patients, ?-synuclein is the major component of the intracellular protein aggregates found in dopaminergic neurons. Previously, short synthetic ?-synuclein-derived peptides have been shown to not only prevent ?-synuclein fibrillation but also dissolve preformed ?-synuclein aggregates in vitro. The hexapeptide PGVTAV was the shortest peptide that retained the ability to block ?-synuclein fibrillation. For preventative or therapeutic effectiveness, a treatment must suppress the neurotoxicity of ?-synuclein aggregates and remain stable in plasma. The present study shows that specific peptides can protect neuronal cells from ?-synuclein aggregation-induced cell death. The ?-sheet-breaking hexapeptide PGVTAV remained intact in human plasma for longer than one day, suggesting that it may be a candidate for the development of therapeutics to treat Parkinson's disease.
PMID: 21510923 [PubMed - indexed for MEDLINE]
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