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

Archive ouverte

Zanyatkin, Ivan | Stroylova, Yulia Yu. | Melnikova, Aleksandra | Moosavi-Movahedi, Ali Akbar | Saboury, Ali Akbar | Haertle, Thomas | Muronetz, Vladimir

Edité par CCSD ; Elsevier -

International audience. 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.

• Description
• Sujet/Public
• Outil
• Outil d'anticipation
• Mémoire et thèse
• Gestion