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

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 200 mm glucose for 48 h 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.