Identifying Biological and Biophysical Features of Different Maturation States of α-Synuclein Amyloid Fibrils.
Methods Mol Biol
; 2551: 321-344, 2023.
Article
em En
| MEDLINE
| ID: mdl-36310213
ABSTRACT
Protein aggregates, hereunder amyloid fibrils, can undergo a maturation process, whereby early formed aggregates undergo a structural and physicochemical transition leading to more mature species. In the case of amyloid-related diseases, such maturation confers distinctive biological properties of the aggregates, which may account for a range of diverse pathological subtypes. Here, we present a protocol for the preparation of α-synuclein amyloid fibrils differing in the level of their maturation. We utilize widely accessible biophysical techniques to characterize the structure and morphology and a simple thermal treatment procedure to test their thermodynamic stability. Their biological properties are probed by means of binding to native plasma membrane sheets originating from mammalian cell lines.
Palavras-chave
Texto completo:
1
Bases de dados:
MEDLINE
Assunto principal:
Alfa-Sinucleína
/
Amiloidose
Limite:
Animals
/
Humans
Idioma:
En
Revista:
Methods Mol Biol
Assunto da revista:
BIOLOGIA MOLECULAR
Ano de publicação:
2023
Tipo de documento:
Article
País de afiliação:
Dinamarca