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Biophys. J. BioFAST: First Published March 31, 2006. doi:10.1529/biophysj.105.079251
© 2006 by the Biophysical Society.

A more recent version of this article appeared on June 15, 2006.
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SPECTROSCOPY, IMAGING, OTHER TECHNIQUES

Quantification of {alpha}-Synuclein binding to lipid vesicles using fluorescence correlation spectroscopy

Elizabeth Rhoades 1, Trudy F. Ramlall 2, Watt W. Webb 1 and David Eliezer 2*

1 Cornell University
2 Weill Medical College of Cornell

* To whom correspondence should be addressed. E-mail: dae2005{at}med.cornell.edu.

Submitted on December 8, 2005
Revised on January 31, 2006
Accepted on 13 March 2006


  Abstract
{alpha}-Synuclein ({alpha}S) is a soluble synaptic protein that is the major proteinaceous component of insoluble fibrillar Lewy body deposits that are the hallmark of Parkinson's disease (PD). The interaction of {alpha}S with synaptic vesicles is thought to be critical both to its normal function as well as to its pathological role in PD. We demonstrate the use of fluorescence correlation spectroscopy (FCS) as a tool for rapid and quantitative analysis of the binding of {alpha}S to large unilamellar vesicles of various lipid compositions. We find that {alpha}S binds preferentially to vesicles containing acidic lipids, and that this interaction can be blocked by increasing the concentration of NaCl in solution. Negative charge is not the only factor determining binding, as we clearly observe binding to vesicles composed entirely of zwitterionic lipids. Additionally, we find enhanced binding to lipids with less bulky head groups. Quantification of the protein to lipid ratio required for binding to different lipid compositions, combined with other data in the literature, yields an upper bound estimate for the number of lipid molecules required to bind each individual molecule of {alpha}S. Our results demonstrate that FCS provides a powerful tool for the quantitative characterization of {alpha}S-lipid interactions.

Key Words: Parkinson's disease, alpha-synuclein, fluorescence correlation spectroscopy, lipid-binding




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Copyright © 2006 by the Biophysical Society.