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Effects of the mutations Ala 30 to Pro and Ala 53 to Thr on the physical and morphological properties of α‐synuclein protein implicated in Parkinson's disease
Author(s) -
El-Agnaf Omar M.A,
Jakes Ross,
Curran Martin D,
Wallace Andrew
Publication year - 1998
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(98)01419-7
Subject(s) - mutant , pathogenesis , mutation , alpha synuclein , amyloid (mycology) , protein aggregation , gene , wild type , parkinson's disease , biology , disease , mutant protein , genetics , medicine , pathology , immunology , botany
α‐Synuclein (α‐syn) protein has been found in association with the pathological lesions of a number of neurodegenerative diseases. Recently, mutations in the α‐syn gene have been reported in families susceptible to an inherited form of Parkinson's disease. We report here that human wild‐type α‐syn, PD‐linked mutant α‐syn(Ala30Pro) and mutant α‐syn(Ala53Thr) proteins can self‐aggregate and form amyloid‐like filaments. The mutant α‐syn forms more β‐sheet and mature filaments than the wild‐type protein. These findings suggest that accumulation of α‐syn as insoluble deposits of amyloid may play a major role in the pathogenesis of these neurodegenerative diseases.