期刊
PRION
卷 7, 期 5, 页码 359-368出版社
LANDES BIOSCIENCE
DOI: 10.4161/pri.26415
关键词
amyloid; fibril; seeding; heteropolymers; polymorph; strain
资金
- Medical Research Council [G0900958] Funding Source: Medline
- Medical Research Council [G0900958] Funding Source: researchfish
- MRC [G0900958] Funding Source: UKRI
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.
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