Secondary structural formation of alpha-synuclein amyloids as revealed by g-factor of solid-state circular dichroism.
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.
Lin
Xiao-Jing
XJ
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.
Zhang
Feng
F
Xie
Yuan-Yuan
YY
Bao
Wen-Jing
WJ
He
Jian-Hua
JH
Hu
Hong-Yu
HY
D000682:Amyloid / Q000737:chemistry; D002942:Circular Dichroism / Q000379:methods*; D006801:Humans; D057927:Hydrophobic and Hydrophilic Interactions; D010300:Parkinson Disease / Q000209:etiology; D010446:Peptide Fragments; D017433:Protein Structure, Secondary; D017550:Spectroscopy, Fourier Transform Infrared; D051844:alpha-Synuclein / Q000737:chemistry*
D000682:Amyloid; D010446:Peptide Fragments; D051844:alpha-Synuclein