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The binding of fisetin to human serum transferrin (HST) was investigated by spectroscopic (steady-state fluorescence, synchronous fluorescence, Förster resonance energy transfer) and molecular docking approaches. HST fluorescence is quenched by fisetin by a static process. The binding takes place with a moderate affinity and it is driven by hydrogen bonding and van der Waals forces. Synchronous fluorescence study indicates that Trp is more involved in the fluorescent quenching of HST by fisetin than Tyr. The energy transfer between HST
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