L17A/F19A substitutions augment the α-helicity of β-amyloid peptide discordant segment

Chu Ting Liang, Hsien Bin Huang, Chih Ching Wang, Yi Ru Chen, Chi Fon Chang*, Ming Shi Shiao, Yi G. Chen, Ta Hsien Lin

*此作品的通信作者

研究成果: Article同行評審

7 引文 斯高帕斯(Scopus)

摘要

β-amyloid peptide (Aβ) aggregation has been thought to be associated with the pathogenesis of Alzheimer's disease. Recently, we showed that L17A/F19A substitutions may increase the structural stability of wild-type and Arctic-type Aβ40 and decrease the rates of structural conversion and fibril formation. However, the underlying mechanism for the increase of structural stability as a result of the alanine substitutions remained elusive. In this study, we apply nuclear magnetic resonance and circular dichroism spectroscopies to characterize the Aβ40 structure, demonstrating that L17A/F19A substitutions can augment the α-helicity of the residues located in the α/β-discordant segment (resides 15 to 23) of both wild-type and Arctic-type Aβ40 . These results provide a structural basis to link the α-helicity of the α/β-discordant segment with the conformational conversion propensity of Aβ.

原文English
文章編號e0154327
期刊PLoS ONE
11
發行號4
DOIs
出版狀態Published - 4月 2016

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