Human serum albumin-resveratrol complex formation: Effect of the phenolic chemical structure on the kinetic and thermodynamic parameters of the interactions

The thermodynamics and kinetics of binding between human serum albumin (HSA) and resveratrol (RES) or its analog (RESAn1) were investigated by surface plasmon resonance (SPR). The binding constant and the kinetic constants of association and dissociation indicated that RESAn1 has higher affinity toward HSA than does RES. The formation of these complexes was entropically driven (TΔS0HSA-RES≅33.8, TΔS0HSA-RESAn1≅56.4 KJ mol−1). However, for both...