title: Study of Protein Amyloid-Like Aggregates by Solid-State Circular Dichroism Spectroscopy.
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.
authors.affiliation: Institute of Biochemistry and Cell Biology, Shanghai Institutes for Biological Sciences, Chinese Academy of Sciences; 320 Yue-Yang Road, Shanghai 200031, China.
authors.forename: Hong-Yu
authors.initials: HY
authors.lastname: Hu
authors.forename: Lei-Lei
authors.initials: LL
authors.lastname: Jiang
authors.forename: Jun-Ye
authors.initials: JY
authors.lastname: Hong
mesh_terms: D000682:Amyloid / Q000737:chemistry* / Q000378:metabolism; D058227:Amyloidogenic Proteins / Q000737:chemistry* / Q000378:metabolism; D002942:Circular Dichroism / Q000379:methods; D006801:Humans; D066329:Protein Aggregates; D011487:Protein Conformation; D013329:Structure-Activity Relationship
chemical_list: D000682:Amyloid; D058227:Amyloidogenic Proteins; D066329:Protein Aggregates