The amyloid stretch hypothesis: recruiting proteins toward the dark side.

ABSTRACT: A detailed understanding of the molecular events underlying the conversion and self-association of normally soluble proteins into amyloid fibrils is fundamental to the identification of therapeutic strategies to prevent or cure amyloid-related disorders. Recent investigations indicate that amyloid fibril formation is not just a general property of the polypeptide backbone depending on external factors, but that it is strongly modulated by amino acid side chains. Here, we propose and address the validation of the premise that the amyloidogenicity of a protein is indeed localized in short protein stretches (amyloid stretch hypothesis). We demonstrate that the conversion of a soluble nonamyloidogenic protein into an amyloidogenic prone molecule can be triggered by a nondestabilizing six-resid

SUBMITTER: Esteras-Chopo A 

PROVIDER: S-EPMC1283810 | biostudies-literature | 2005 Nov

REPOSITORIES: biostudies-literature