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Current Protein & Peptide Science

Editor-in-Chief

ISSN (Print): 1389-2037
ISSN (Online): 1875-5550

Review Article

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

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

Volume 18, Issue 1, 2017

Page: [100 - 103] Pages: 4

DOI: 10.2174/1389203717666160709185323

Price: $65

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.

Graphical Abstract

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