The newly discovered Parkinson's disease associated Finnish mutation (A53E) attenuates α-synuclein aggregation and membrane binding.

Abstract:

:α-Synuclein (α-Syn) oligomerization and amyloid formation are associated with Parkinson's disease (PD) pathogenesis. Studying familial α-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 α-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.

journal_name

Biochemistry

journal_title

Biochemistry

authors

Ghosh D,Sahay S,Ranjan P,Salot S,Mohite GM,Singh PK,Dwivedi S,Carvalho E,Banerjee R,Kumar A,Maji SK

doi

10.1021/bi5010365

subject

Has Abstract

pub_date

2014-10-21 00:00:00

pages

6419-21

issue

41

eissn

0006-2960

issn

1520-4995

journal_volume

53

pub_type

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