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

Author(s): Hong-Yu Hu, Lei-Lei Jiang, Jun-Ye Hong

Journal Name: Current Protein & Peptide Science

Volume 18 , Issue 1 , 2017

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Graphical 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.

Keywords: Circular dichroism, Solid state, Protein amyloid, Secondary structure, Structural transformation.

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Article Details

Year: 2017
Published on: 09 November, 2016
Page: [100 - 103]
Pages: 4
DOI: 10.2174/1389203717666160709185323
Price: $65

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