Assessing the causes and consequences of co-polymerization in amyloid formation.
Prion
; 7(5): 359-68, 2013.
Article
em En
| MEDLINE
| ID: mdl-24025483
ABSTRACT
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., ß2-microglobulin and ΔN6, Aß40, and Aß42), sequence variants (e.g., Aß and Aß(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.
Palavras-chave
Texto completo:
1
Base de dados:
MEDLINE
Assunto principal:
Precursores de Proteínas
/
Microglobulina beta-2
/
Proteínas Mutantes
/
Amiloide
Tipo de estudo:
Etiology_studies
Limite:
Humans
Idioma:
En
Ano de publicação:
2013
Tipo de documento:
Article