Secondary structural formation of alpha-synuclein amyloids as revealed by g-factor of solid-state circular dichroism.

Abstract:

:Alpha-synuclein (alpha-Syn) has been identified as a component of intracellular fibrillar deposits in Parkinson's disease. Though the real pathogenesis is still unknown, many investigations have revealed that conformational alteration and fibril formation of alpha-Syn protein have an important role in causing the disease. In this work, we introduced the g-factor spectra of solid-state circular dichroism to estimate the secondary structure contents of alpha-Syn fragments in amyloids. Fourier-transform infrared (FTIR) was also applied to confirm the structural formation. The results suggest that the central hydrophobic region is critical for beta-sheet formation and the conformational alteration is the foundation of protein abnormal aggregation. The research provides a practical approach to estimate the secondary structure contents of protein amyloids and further insight into the relevance of structural transformation and amyloidogenesis.

journal_name

Biopolymers

journal_title

Biopolymers

authors

Lin XJ,Zhang F,Xie YY,Bao WJ,He JH,Hu HY

doi

10.1002/bip.20550

subject

Has Abstract

pub_date

2006-10-15 00:00:00

pages

226-32

issue

3

eissn

0006-3525

issn

1097-0282

journal_volume

83

pub_type

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