Structure and intermolecular dynamics of aggregates populated during amyloid fibril formation studied by hydrogen/deuterium exchange.

Journal article

The aggregation of proteins into amyloid fibrils is a complex and fascinating process associated with debilitating clinical disorders such as Alzheimer's and Parkinson's diseases. The process of aggregation involves a series of steps during which many intermediate aggregation states are populated. Recent evidence points to these intermediate states as the toxic moieties primarily responsible for cell damage or cell death, which are critical steps in the origin and progression of these disorde...

Expand abstract

Authors: Carulla, N; Zhou, M; Giralt, E; Robinson, C; Dobson, C

• Publication status: Published
• Journal: Accounts of chemical research
• Volume: 43
• Issue: 8
• Pages: 1072-1079
• Publication date: 2010-08-01
• DOI: 10.1021/ar9002784
• EISSN: 1520-4898
• ISSN: 0001-4842
• Language: English
• Keywords: Humans; Peptides; Protein Conformation; Amyloid; Amyloid beta-Peptides; Amino Acid Sequence; Kinetics; Proteins; Deuterium; Solvents; Alzheimer Disease; Amyloidosis; Hydrogen