aDepartment of Bioengineering and Bioinformatics, M.V. Lomonosov Moscow State University, Moscow, Russian Federation bA.N. Belozersky Research Institute of Physico-Chemical Biology, M.V. Lomonosov Moscow State University, Moscow, Russian Federation cInstitute of Molecular Medicine, I.M. Sechenov First Moscow
State Medical University, Moscow, Russian Federation dInstitute of Biochemistry and Biophysics, University of Tehran, Tehran, Iran eBiopolymers, Interactions, Assemblies, UR 1268, Institute National de la Recherche Agronomique, Nantes, France fDepartment of Animal Nutrition, Poznan University of Life Sciences, Poznan, Poland
Аннотация:
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.
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