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The Parkinson's Disease-Associated H50Q Mutation Accelerates alpha-Synuclein Aggregation in Vitro

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Title The Parkinson's Disease-Associated H50Q Mutation Accelerates alpha-Synuclein Aggregation in Vitro
 
Creator GHOSH, D
MONDAL, M
MOHITE, GM
SINGH, PK
RANJAN, P
ANOOP, A
GHOSH, S
JHA, NN
KUMAR, A
MAJI, SK
 
Subject FREE-ENERGY LANDSCAPES
WILD-TYPE
PROTEIN
DYNAMICS
IMPACT
 
Description alpha-Synuclein (alpha-Syn) aggregation is directly linked with Parkinson's disease (PD) pathogenesis. Here, we analyzed the aggregation of newly discovered a-Syn missense mutant H50Q in vitro and found that this mutation significantly accelerates the aggregation and amyloid formation of alpha-Syn. This mutation, however, did not alter the overall secondary structure as suggested by two-dimensional nuclear magnetic resonance and circular dichroism spectroscopy. The initial oligomerization study by cross-linking and chromatographic techniques suggested that this mutant oligomerizes to an extent similar to that of the wild-type alpha-Syn protein. Understanding the aggregation mechanism of this H50Q mutant may help to establish the aggregation and phenotypic relationship of this novel mutant in PD.
 
Publisher AMER CHEMICAL SOC
 
Date 2014-10-16T13:38:05Z
2014-10-16T13:38:05Z
2013
 
Type Article
 
Identifier BIOCHEMISTRY, 52(40)6925-6927
0006-2960
1943-295X
http://dx.doi.org/10.1021/bi400999d
http://dspace.library.iitb.ac.in/jspui/handle/100/15685
 
Language en