Assessing the causes and consequences of co-polymerization in amyloid formation

作者：Sarell Claire J; Stockley Peter G; Radford Sheena E^*

来源：Prion, 2013, 7(5): 359-368.

DOI：10.4161/pri.26415

• amyloid
• fibril
• seeding
• heteropolymers
• polymorph
• strain

How, and why, different proteins form amyloid fibrils is most often studied in vitro using a single purified protein sequence. However, many amyloid diseases involve co-aggregation of different protein species, including proteins with/without post-translational modifications (e.g., different strains of PrP), proteins of different length (e.g., (2)-microglobulin and N6, A40, and A42), sequence variants (e.g., A and A(ARC)), and proteins from different organisms (e.g., bovine PrP and human PrP). The consequences of co-aggregation of different proteins upon the structure, stability, species transmission and toxicity of the resulting amyloid aggregates is discussed here, including the role of co-aggregation in expanding the repertoire of oligomeric and fibrillar structures and how this can affect their biological and biophysical properties.

• 出版日期2013-9-1