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

✍ Scribed by Xiao-Jing Lin; Feng Zhang; Yuan-Yuan Xie; Wen-Jing Bao; Jian-Hua He; Hong-Yu Hu

• Publisher: Wiley (John Wiley & Sons)
• Year: 2006
• Tongue: English
• Weight: 255 KB
• Volume: 83
• Category: Article
• ISSN: 0006-3525
• DOI: 10.1002/bip.20550

✦ Synopsis

Abstract

α‐Synuclein (α‐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 α‐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 α‐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 β‐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. © 2006 Wiley Periodicals, Inc. Biopolymers 83: 226–232, 2006

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