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KMID : 0603820120180040329
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Journal of Experimental & Biomedical Science
2012 Volume.18 No. 4 p.329 ~ p.337
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Macromolecular Crowding Enhances Interaction of α-synuclein with Vesicles
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Kim Yoon-Suk
Kim Jeong-han
Yi Chi-A
Ko Je-Sang
Park Yong-Serk
Lee Seung-Jae
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Abstract
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α-synuclein (α-syn) is known to be implicated in the pathogenesis of Parkinson"s disease and transiently bind to biological vesicles. In this study, we examined the effect of molecular crowding on the interaction of α-syn with biological vesicles by using inert polymers since the environment of proteins in cells are crowded with other macromolecules. The addition of different polymers including polyethylene glycol, dextran, and ficoll enhanced the binding of α-syn to vesicles in a concentration-dependent manner and the association of α-syn with vesicle was proportionally augmented by increased expression of α-syn. However, molecular crowding had a neglectable effect on the vesicle binding of α-syn mutants (A30P, TG6), which has been reported to show impaired vesicle binding capacity. These results suggest that transient interaction of α-syn with vesicles occurs more commonly in cells than expected implying interaction with vesicles may be one of the physiological processes in which α-syn is involved.
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KEYWORD
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Alpha-synuclein, Vesicles, Macromolecular crowding, Parkinson's disease
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