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Characterization of fibrillation process of alpha-synuclein at the initial stage.

Abstract：

:alpha-Synuclein is the major component of the filamentous Lewy bodies and Lewy-related neurites, neuropathological hallmarks of Parkinson's disease. Although numerous studies on alpha-synuclein fibrillation have been reported, the molecular mechanisms of aggregation and fibrillation at the initial stage are still unclear. In the present study, structural properties and propensities to form fibrils of alpha-synuclein at the initial stage were investigated using 2D (1)H-(15)N NMR spectroscopy, electron microscope, and small angle X-ray scattering (SAXS). Observation of the 2D (1)H-(15)N HSQC spectra indicated significant attenuation of many cross peak intensities in the regions of KTKEGV-type repeats and the non-Abeta component of Alzheimer's disease amyloid (NAC), suggesting that these regions contributed fibril formation. Oligomerization comprising heptamer was successfully monitored at the initial stage using the time-dependent SAXS measurements.

journal_name

Biochem Biophys Res Commun

journal_title

Biochemical and biophysical research communications

authors

Tashiro M,Kojima M,Kihara H,Kasai K,Kamiyoshihara T,Uéda K,Shimotakahara S

doi

10.1016/j.bbrc.2008.02.127

subject

Has Abstract

pub_date

2008-05-09 00:00:00

pages

910-4

issue

3

eissn

0006-291X

issn

1090-2104

pii

S0006-291X(08)00399-9

journal_volume

369

pub_type

杂志文章

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