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alpha-Synuclein Adopts an alpha-Helical Conformation in the Presence of Polyunsaturated Fatty Acids To Hinder Micelle Formation.

Broersen K, Brink DV, Fraser G, Goedert M, Davletov B

MRC Laboratory of Molecular Biology, Hills Road, Cambridge CB2 2QH, U.K.

&agr;-Synuclein is a small cytosolic protein involved in the pathogenesis of Parkinson's disease and other neurodegenerative disorders. Recent studies suggested a lipid-related function for this brain-enriched protein. Since the brain carries a high level of docosahexaenoic acid (DHA) and since the extent of &agr;-synuclein gene expression increases in response to DHA intake, we have investigated the interaction of &agr;-synuclein with this essential omega-3 fatty acid. We show that &agr;-synuclein allows DHA to be present in a soluble rather than micellar form. Upon interaction with DHA, the normally unstructured &agr;-synuclein rapidly adopts an &agr;-helical conformation. Prolonged exposure to DHA, however, gradually converts &agr;-synuclein into amyloid-like fibrils. These results identify a potential biological function for &agr;-synuclein and define an omega-3-linked pathway leading to &agr;-synuclein aggregation.

Published 19 December 2006 in Biochemistry, 45(51): 15610-15616.
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