title: beta-sheet structure formation of proteins in solid state as revealed by circular dichroism spectroscopy.
abstract: Cross beta-sheet structure formation and abnormal aggregation of proteins are thought to be pathological characteristics of some neurodegenerative disorders. To investigate the novel structural transformation and aggregation, the solid-state secondary structures of some proteins and peptides associated in thin films were determined by circular dichroism spectroscopy. Insulin, lysozyme, DsbA protein, luciferase, and ovalbumin peptide fall into one group; they show no or slight structural rearrangement from solution to the solid state. Another group, including bovine serum albumin, ovalbumin, alpha-synuclein, and plasminogen activator inhibitor-1 (PAIRC) peptide, undergo structural transformation with an increase of beta-sheet structure in the solid state. The beta-sheet formation of PAIRC peptide may reflect the structural transformation of the serpin reactive center that is relevant to the inhibitor activity. The beta-sheet structure of alpha-synuclein in the solid state may correspond to the amyloid-like aggregates, which are implicated in the pathogenesis of some neurodegenerative diseases.
authors.affiliation: Shanghai Institute of Biochemistry, Chinese Academy of Sciences, Shanghai 200031, People's Republic of China. hyhu@sunm.shcnc.ac.cn
authors.forename: H Y
authors.initials: HY
authors.lastname: Hu
authors.forename: Q
authors.initials: Q
authors.lastname: Li
authors.forename: H C
authors.initials: HC
authors.lastname: Cheng
authors.forename: H N
authors.initials: HN
authors.lastname: Du
mesh_terms: D016229:Amyloid beta-Peptides / Q000737:chemistry; D000818:Animals; D002417:Cattle; D002942:Circular Dichroism; D004195:Disease Models, Animal; D007328:Insulin / Q000737:chemistry; D008156:Luciferases / Q000737:chemistry; D008958:Models, Molecular; D009113:Muramidase / Q000737:chemistry; D009419:Nerve Tissue Proteins / Q000737:chemistry; D010047:Ovalbumin / Q000737:chemistry; D017395:Plasminogen Activator Inhibitor 1 / Q000737:chemistry; D011487:Protein Conformation; D019704:Protein Disulfide-Isomerases / Q000737:chemistry; D017433:Protein Structure, Secondary; D012710:Serum Albumin, Bovine / Q000737:chemistry; D013057:Spectrum Analysis / Q000295:instrumentation / Q000379:methods; D013329:Structure-Activity Relationship; D051843:Synucleins; D051844:alpha-Synuclein
chemical_list: D016229:Amyloid beta-Peptides; D007328:Insulin; D009419:Nerve Tissue Proteins; D017395:Plasminogen Activator Inhibitor 1; D051843:Synucleins; D051844:alpha-Synuclein; D012710:Serum Albumin, Bovine; D010047:Ovalbumin; D008156:Luciferases; D009113:Muramidase; D019704:Protein Disulfide-Isomerases