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The Newly Discovered Parkinson's Disease Associated Finnish Mutation (A53E) Attenuates alpha-Synuclein Aggregation and Membrane Binding

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Title The Newly Discovered Parkinson's Disease Associated Finnish Mutation (A53E) Attenuates alpha-Synuclein Aggregation and Membrane Binding
 
Creator GHOSH, D
SAHAY, S
RANJAN, P
SALOT, S
MOHITE, GM
SINGH, PK
DWIVEDI, S
CARVALHO, E
BANERJEE, R
KUMAR, A
MAJI, SK
 
Subject FIBRIL FORMATION
IN-VITRO
 
Description alpha-Synuclein (a-Syn) oligomerization and amyloid formation are associated with Parkinson's disease (PD) pathogenesis. Studying familial a-Syn mutants associated with early onset PD has therapeutic importance. Here we report the aggregation kinetics and other biophysical properties of a newly discovered PD associated Finnish mutation (A53E). Our in vitro study demonstrated that A53E attenuated a-Syn aggregation and amyloid formation without altering the major secondary structure and initial oligomerization tendency. Further, A53E showed reduced membrane binding affinity compared to A53T and WT. The present study would help to delineate the role of A53E mutation in early onset PD pathogenesis.
 
Publisher AMER CHEMICAL SOC
 
Date 2014-12-29T05:35:43Z
2014-12-29T05:35:43Z
2014
 
Type Article
 
Identifier BIOCHEMISTRY, 53(41)6419-6421
0006-2960
http://dx.doi.org/10.1021/bi5010365
http://dspace.library.iitb.ac.in/jspui/handle/100/17208
 
Language English