Formation of distinct prion protein amyloid fibrils under identical experimental conditions.
Sci Rep
; 10(1): 4572, 2020 03 12.
Article
em En
| MEDLINE
| ID: mdl-32165692
ABSTRACT
Protein aggregation into amyloid fibrils is linked to multiple neurodegenerative disorders, such as Alzheimer's, Parkinson's or Creutzfeldt-Jakob disease. A better understanding of the way these aggregates form is vital for the development of drugs. A large detriment to amyloid research is the ability of amyloidogenic proteins to spontaneously aggregate into multiple structurally distinct fibrils (strains) with different stability and seeding properties. In this work we show that prion proteins are capable of forming more than one type of fibril under the exact same conditions by assessing their Thioflavin T (ThT) binding ability, morphology, secondary structure, stability and seeding potential.
Texto completo:
1
Base de dados:
MEDLINE
Assunto principal:
Benzotiazóis
/
Proteínas Priônicas
Limite:
Animals
Idioma:
En
Ano de publicação:
2020
Tipo de documento:
Article