Binding with nucleic acids or glycosaminoglycans converts soluble protein oligomers to amyloid.

ABSTRACT: Ample evidence suggests that almost all polypeptides can either adopt a native structure (folded or intrinsically disordered) or form misfolded amyloid fibrils. Soluble protein oligomers exist as an intermediate between these two states, and their cytotoxicity has been implicated in the pathology of multiple human diseases. However, the mechanism by which soluble protein oligomers develop into insoluble amyloid fibrils is not clear, and investigation of this important issue is hindered by the unavailability of stable protein oligomers. Here, we have obtained stabilized protein oligomers generated from common native proteins. These oligomers exert strong cytotoxicity and display a common conformational structure shared with known protein oligomers. They are soluble and remain stable in solu

SUBMITTER: Di Domizio J 

PROVIDER: S-EPMC3249128 | biostudies-literature | 2012 Jan

REPOSITORIES: biostudies-literature