β-Sheet structure formation of proteins in solid state as revealed by circular dichroism spectroscopy

✍ Scribed by Hong-Yu Hu; Qi Li; Hong-Chang Cheng; Hai-Ning Du

• Publisher: Wiley (John Wiley & Sons)
• Year: 2000
• Tongue: English
• Weight: 173 KB
• Volume: 62
• Category: Article
• ISSN: 0006-3525
• DOI: 10.1002/1097-0282(2001)62:1<15::aid-bip30>3.0.co;2-j

✦ Synopsis

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.