%0 Journal Article
%A Ghosh, Dhiman
%A Mondal, Mrityunjoy
%A Mohite, Ganesh
M.
%A Singh, Pradeep
K.
%A Ranjan, Priyatosh
%A Anoop, A.
%A Ghosh, Saikat
%A Jha, Narendra Nath
%A Kumar, Ashutosh
%A Maji, Samir K.
%D 2013
%T The Parkinson’s Disease-Associated H50Q Mutation
Accelerates α‑Synuclein Aggregation in Vitro
%U https://acs.figshare.com/articles/journal_contribution/The_Parkinson_s_Disease_Associated_H50Q_Mutation_Accelerates_Synuclein_Aggregation_i_in_Vitro_i_/2368417
%R 10.1021/bi400999d.s001
%2 https://acs.figshare.com/ndownloader/files/4007869
%K H 50Q
%K Syn
%K mutation
%K PD
%K aggregation
%K Parkinson
%X α-Synuclein (α-Syn) aggregation
is directly linked
with Parkinson’s disease (PD) pathogenesis. Here, we analyzed
the aggregation of newly discovered α-Syn missense mutant H50Q in vitro and found that this mutation significantly accelerates
the aggregation and amyloid formation of α-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 α-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.
%I ACS Publications