Aβ40(L17A/F19A) mutant diminishes the aggregation and neurotoxicity of Aβ40

Yi Ru Chen, Hsien Bin Huang, Chi Jen Lo, Chih Ching Wang, Chia Li Su, Hsin Tzu Liu, Ming Shi Shiao, Ta Hsien Lin*, Yi Chen Chen

*此作品的通信作者

研究成果: Article同行評審

11 引文 斯高帕斯(Scopus)

摘要

Aggregated β-amyloid peptides (Aβ) are neurotoxic and responsible for neuronal death both in vitro and in vivo. From the structural point of view, Aβ self-aggregation involves a conformational change in the peptide. Here, we investigated the relationship between conformational changes and amino acid residues of Aβ40. Urea unfolding in combination with NMR spectroscopy was applied to probe the stabilization of Aβ40 conformation. L17 and F19 residues were found more sensitive to environmental changes than the other residues. Replacement of these two residues with alanine could stabilize the conformation of Aβ40. Further analysis indicated that the Aβ40(L17A/F19A) mutant could diminish the aggregation and reduce the neurotoxicity. These results suggest that L17 and F19 are the critical residues responsible for conformational changes which may trigger neurotoxic cascade of Aβ40.

原文English
頁(從 - 到)91-95
頁數5
期刊Biochemical and Biophysical Research Communications
405
發行號1
DOIs
出版狀態Published - 4 2月 2011

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