A common beta-sheet architecture underlies in vitro and in vivo beta2-microglobulin amyloid fibrils.

ABSTRACT: Misfolding and aggregation of normally soluble proteins into amyloid fibrils and their deposition and accumulation underlies a variety of clinically significant diseases. Fibrillar aggregates with amyloid-like properties can also be generated in vitro from pure proteins and peptides, including those not known to be associated with amyloidosis. Whereas biophysical studies of amyloid-like fibrils formed in vitro have provided important insights into the molecular mechanisms of amyloid generation and the structural properties of the fibrils formed, amyloidogenic proteins are typically exposed to mild or more extreme denaturing conditions to induce rapid fibril formation in vitro. Whether the structure of the resulting assemblies is representative of their natural in vivo counterparts, thus, r

SUBMITTER: Jahn TR 

PROVIDER: S-EPMC2427364 | biostudies-literature | 2008 Jun

REPOSITORIES: biostudies-literature