Protein aggregation diseases.
Amyloidosis defines a group of protein misfolding diseases, and today more than 30 different proteins have been characterized as amyloid forming in man. Despite sequence differences the peptides assemble into long slender fibrils with a similar morphological appearance. Propagation of amyloid fibrils is believed to involve the formation of smaller cell-toxic species that trigger cell death. In addition to this mechanism the amyloid mass may be extensive and destroy the cellular architecture of an organ. We study different aspects on amyloid, from initiation of fibrillation, toxicity of different fibrils and endogenous clearance of amyloid.