Study on the interaction of fisetholz with BSA/HSA by multi-spectroscopic, cyclic voltammetric, and molecular docking technique.

The interaction of fisetholz with bovine serum albumin (BSA) and human serum albumin (HSA) was investigated by multi-spectroscopic, cyclic voltammetric, and molecular docking technique. The results revealed that there was a static quenching of BSA/HSA induced by fisetholz. The binding constants () and binding sites () were calculated at different temperatures (293, 303, and 311 K).