Unusual spiral structures formed by glycated β-casein in the presence of thioflavin T: amyloid transformation? - INRAE - Institut national de recherche pour l’agriculture, l’alimentation et l’environnement Accéder directement au contenu
Article Dans Une Revue Mendeleev Communications Année : 2021

Unusual spiral structures formed by glycated β-casein in the presence of thioflavin T: amyloid transformation?

Résumé

Unusual spiral-like structures in aggregates formed by beta-casein glycated in a special way in the presence of thioflavin T are reported. Different glycation agents, temperature, pH, incubation time, and concentrations of protein and modifier were characterized, but only glycated by 200 mM glucose for 48 h at 37 degrees C without sodium cyanoborohydride beta-casein forms spiral structures in the presence of thioflavin T. Thioflavin T affects the size of particles formed by glycated beta-casein and also stimulates heat-induced aggregation, indicating that the formation of unusual spiral structures is determined both by the structure of the advanced glycation end products and by the properties of the glycated protein.
Fichier non déposé

Dates et versions

hal-03252595 , version 1 (07-06-2021)

Identifiants

Citer

Ivan Zanyatkin, Yulia Yu. Stroylova, Aleksandra Melnikova, Ali Akbar Moosavi-Movahedi, Ali Akbar Saboury, et al.. Unusual spiral structures formed by glycated β-casein in the presence of thioflavin T: amyloid transformation?. Mendeleev Communications, 2021, 31 (1), pp.73-75. ⟨10.1016/j.mencom.2021.01.022⟩. ⟨hal-03252595⟩

Collections

INRAE
13 Consultations
0 Téléchargements

Altmetric

Partager

Gmail Facebook X LinkedIn More