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Biochim Biophys Acta. 2012 Feb;1822(2):261-85. doi: 10.1016/j.bbadis.2011.10.002. Epub 2011 Oct 12.

Α-synuclein misfolding and Parkinson's disease.

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1
Department of Molecular Medicine, College of Medicine, University of South Florida, Tampa, FL 33612, USA.

Abstract

Substantial evidence links α-synuclein, a small highly conserved presynaptic protein with unknown function, to both familial and sporadic Parkinson's disease (PD). α-Synuclein has been identified as the major component of Lewy bodies and Lewy neurites, the characteristic proteinaceous deposits that are the hallmarks of PD. α-Synuclein is a typical intrinsically disordered protein, but can adopt a number of different conformational states depending on conditions and cofactors. These include the helical membrane-bound form, a partially-folded state that is a key intermediate in aggregation and fibrillation, various oligomeric species, and fibrillar and amorphous aggregates. The molecular basis of PD appears to be tightly coupled to the aggregation of α-synuclein and the factors that affect its conformation. This review examines the different aggregation states of α-synuclein, the molecular mechanism of its aggregation, and the influence of environmental and genetic factors on this process.

PMID:
22024360
DOI:
10.1016/j.bbadis.2011.10.002
[Indexed for MEDLINE]
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