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

Abstract : 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.
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https://hal.inrae.fr/hal-03252595
Contributor : Olivier Dupre <>
Submitted on : Monday, June 7, 2021 - 5:25:55 PM
Last modification on : Monday, June 7, 2021 - 5:25:58 PM

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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, Elsevier, 2021, 31 (1), pp.73-75. ⟨10.1016/j.mencom.2021.01.022⟩. ⟨hal-03252595⟩

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