Abstract
The interaction of vitamins C, B12, and folic acid (B9) with human serum transferrin (HST) was studied. A static interaction mechanism for the binding of the vitamins with HST was revealed. The interaction takes place with small binding constants in the case of both vitamin C and B12, and a moderate constant in the case of folic acid. The driving forces of the interactions were: hydrophobic for vitamin B12, hydrogen bonding and van der Waals forces for vitamin C, and electrostatic forces for the folic acid. The microenvironments of its fluorescent amino acids, Trp and Tyr, were changed by all bound vitamins. The distances between HST and vitamins were determined, these data confirming the results obtained by fluorescence experiments. The denaturation temperature of HST was modified by the interactions with vitamins. Molecular docking simulation showed the best orientation of vitamins towards HST 3D structure and confirmed the fluorescence data.
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