Abstract HTML Views: 632 PDF Downloads: 299 Total Views/Downloads: 1044
Abstract HTML Views: 421 PDF Downloads: 226 Total Views/Downloads: 739
The misfolding and aggregation of proteins into amyloid has been linked to a variety of age-related diseases.
Aggregation of proteins, such as Aβ in Alzheimer's disease and Islet Amyloid Polypeptide (IAPP, amylin) in type 2 diabetes,
appears to lead to the formation of toxic assemblies. These assemblies range in size from small oligomers (2-8 proteins)
to large fibrils (thousands of proteins). It remains unclear how these amyloidogenic proteins misfold and form toxic
species, but growing evidence suggests that inhibiting the aggregation of these proteins could slow, if not prevent altogether,
the progression of these diseases. We describe the use of small peptides (<43 amino acids) as inhibitors of amyloid-
based aggregation. These peptides, often short complementary segments of the amyloid proteins, can be useful (i) for
identifying the aggregation-prone regions of the amyloid proteins (ii) as models for drug discovery and (iii) as potential
therapeutic agents themselves.