Superoxide dismutase-1 alters the rate of prion protein aggregation and resulting fibril conformation.
Arch Biochem Biophys
; 715: 109096, 2022 01 15.
Article
em En
| MEDLINE
| ID: mdl-34848178
ABSTRACT
The assembly of amyloidogenic proteins into highly-structured fibrillar aggregates is related to the onset and progression of several amyloidoses, including neurodegenerative Alzheimer's or Parkinson's diseases. Despite years of research and a general understanding of the process of such aggregate formation, there are currently still very few drugs and treatment modalities available. One of the factors that is relatively insufficiently understood is the cross-interaction between different amyloid-forming proteins. In recent years, it has been shown that several of these proteins or their aggregates can alter each other's fibrillization properties, however, there are still many unknowns in the amyloid interactome. In this work, we examine the interaction between amyloid disease-related prion protein and superoxide dismutase-1. We show that not only does superoxide dismutase-1 increase the lag time of prion protein fibril formation, but it also changes the conformation of the resulting aggregates.
Palavras-chave
Texto completo:
1
Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Fragmentos de Peptídeos
/
Agregados Proteicos
/
Superóxido Dismutase-1
/
Proteínas Priônicas
Limite:
Animals
Idioma:
En
Ano de publicação:
2022
Tipo de documento:
Article