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JOURNALS // Mendeleev Communications // Archive
Mendeleev Commun., 2021 Volume 31, Issue 1, Pages 73–75 (Mi mendc838)
This article is cited in 2 papers

Communications

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

I. A. Zanyatkina, Yu. Yu. Stroylovabc, A. K. Melnikovaa, A. A. Moosavi-Movahedid, A. A. Sabouryd, T. Haertleef, V. I. Muronetzab

a Department of Bioengineering and Bioinformatics, M.V. Lomonosov Moscow State University, Moscow, Russian Federation
b A.N. Belozersky Research Institute of Physico-Chemical Biology, M.V. Lomonosov Moscow State University, Moscow, Russian Federation
c Institute of Molecular Medicine, I.M. Sechenov First Moscow State Medical University, Moscow, Russian Federation
d Institute of Biochemistry and Biophysics, University of Tehran, Tehran, Iran
e Biopolymers, Interactions, Assemblies, UR 1268, Institute National de la Recherche Agronomique, Nantes, France
f Department of Animal Nutrition, Poznan University of Life Sciences, Poznan, Poland

Abstract: Unusual spiral-like structures in aggregates formed by β-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 200mm glucose for 48h at 37°C without sodium cyanoborohydride β-casein forms spiral structures in the presence of thioflavin T. Thioflavin T affects the size of particles formed by glycated β-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.

Keywords: β-casein, thioflavin T, amyloid structure, aggregation, protein glycation, advanced glycation end-products.

Language: English

DOI: 10.1016/j.mencom.2021.01.022


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