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Engineered alpha-synuclein prevents wild type and familial Parkin variant fibril formation.

Abstract：

:Alpha-synuclein is a major component of several pathological lesions diagnostic of specific neurodegenerative disease such as Parkinson's disease. This study focuses on the non-amyloid beta component of Alzheimer's disease amyloid, a key region for the aggregation and fibril formation of alpha-synuclein. Several mutations were introduced in an attempt to repress beta-strand formation and hydrophobic interaction-based aggregation. Although reducing the hydrophobicity drastically decreased fibril formation, the Val70Thr and Val70Pro mutations resulted in an unstable secondary structure thereby increasing non-structural aggregation, instead of fibril formation. Therefore, the stabilization of non-structural natively unfolded status is important to prevent alpha-synuclein fibril formation. Mixing the Val70Thr/Val71Thr double mutant, which has inherently low potential, with the fibril forming alpha-synucleins, WT and Ala53Thr, greatly reduced their fibril formation and aggregation. This double mutant has great potential for further therapeutic approaches.

journal_name

Biochem Biophys Res Commun

journal_title

Biochemical and biophysical research communications

authors

Sode K,Usuzaka E,Kobayashi N,Ochiai S

doi

10.1016/j.bbrc.2005.07.100

subject

Has Abstract

pub_date

2005-09-23 00:00:00

pages

432-6

issue

2

eissn

0006-291X

issn

1090-2104

pii

S0006-291X(05)01587-1

journal_volume

335

pub_type

杂志文章

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