Secondary structural formation of alpha-synuclein amyloids as revealed by g-factor of solid-state circular dichroism |
| |
Authors: | Lin Xiao-Jing Zhang Feng Xie Yuan-Yuan Bao Wen-Jing He Jian-Hua Hu Hong-Yu |
| |
Affiliation: | Key Laboratory of Proteomics, Institute of Biochemistry and Cell Biology, Shanghai Institutes for Biological Sciences, Chinese Academy of Sciences, 320 Yue-yang Road, Shanghai 200031, China. |
| |
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. |
| |
Keywords: | α‐synuclein circular dichroism g‐factor aggregation GAV motif FTIR |
本文献已被 PubMed 等数据库收录! |
|