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Nanomedicine. 2008 Dec;4(4):350-7. doi: 10.1016/j.nano.2008.05.005. Epub 2008 Jul 18.

Mechanism of alpha-synuclein oligomerization and membrane interaction: theoretical approach to unstructured proteins studies.

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  • 1Department of Chemistry and Biochemistry, University of California San Diego, La Jolla, California 92093-0444, USA. itsigeln@ucsd.edu

Abstract

Misfolding and oligomerization of unstructured proteins is involved in the pathogenesis of Parkinson's disease (PD), Alzheimer's disease, Huntington's disease, and other neurodegenerative disorders. Elucidation of possible conformations of these proteins and their interactions with the membrane is necessary to understand the molecular mechanisms of neurodegeneration. We developed a strategy that makes it possible to elucidate the molecular mechanisms of alpha-synuclein aggregation-a key molecular event in the pathogenesis of PD. This strategy can be also useful for the study of other unstructured proteins involved in neurodegeneration. The results of these theoretical studies have been confirmed with biochemical and electrophysiological studies. Our studies provide insights into the molecular mechanism for PD initiation and progression, and provide a useful paradigm for identifying possible therapeutic interventions through computational modeling.

PMID:
18640077
PMCID:
PMC2627560
DOI:
10.1016/j.nano.2008.05.005
[PubMed - indexed for MEDLINE]
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