ABSTRACT
A number of diseases are associated with the pathological aggregation of normally soluble proteins and the deposition of these aggregates in the form of amyloid plaques on various organs on the body. More than 20 such amyloid diseases, including Parkinson’s and Alzheimer’s diseases, have been identi-ed [1,2]. e proteins involved in amyloid disorders are varied in terms of sequence and native fold, yet they self-assemble via similar nucleation-growth kinetics to a similar end product, a cross-β bril with characteristic properties, including the ability to bind to amyloidogenic dyes. Importantly, even proteins that are not naturally associated with amyloidosis can form bers under conditions that destabilize the native fold. A number of short peptides have also been shown to aggregate readily under concentrated conditions, and certain organisms utilize the aggregation process for functional purposes, such as scaolding in bacteria [3]. ese observations suggest that the formation of amyloid bers is a common feature of all proteins [1].
