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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 and fisetin occurs at a distance of 2.31 nm confirming the results obtained by fluorescence. The binding of fisetin to HST favors thermal denaturation of HST conformation. The transition temperature for HST was obtained at 53.81 while the presence of the fisetin led to its change to 49.06 The molecular docking of fisetin to HST confirms the results obtained by the spectroscopic experiments showing a moderate affinity of fisetin for HST. Communicated by Ramaswamy H. Sarma

Probing the interaction of fisetin with human serum transferrin via spectroscopic and molecular docking approaches