Study of Protein Amyloid-Like Aggregates by Solid-State Circular Dichroism Spectroscopy.

Curr Protein Pept Sci

Institute of Biochemistry and Cell Biology, Shanghai Institutes for Biological Sciences, Chinese Academy of Sciences; 320 Yue-Yang Road, Shanghai 200031, China.

Published: February 2017

AI Article Synopsis

  • Protein aggregation and the formation of amyloid fibrils play a critical role in the development of neurodegenerative diseases.
  • Understanding the structure and shape of these amyloid aggregates is essential for grasping the underlying molecular processes of related disorders.
  • This review article focuses on the principles of solid-state circular dichroism (ssCD) spectroscopy and its application in analyzing the secondary structures of proteins and peptides as they undergo amyloidogenic aggregation.

Article Abstract

Protein aggregation and amyloidogenesis are closely associated with the pathogenesis of neurodegenerative diseases. Elucidating the morphology and structure of the amyloid aggregates or fibrils is important for understanding the molecular mechanisms of these proteinopathies. This review article describes the general principle and establishment of solid-state circular dichroism (ssCD) spectroscopy, and discusses its application for the analysis of secondary structures of proteins or peptides in amyloids and structural transformation of these proteins or peptides during their amyloidogenic aggregation.

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http://dx.doi.org/10.2174/1389203717666160709185323DOI Listing

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