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

•Resveratrol (RES) and its analog RESAn1 form complexes with human serum albumin (HSA).•Polyphenol structure influenced the thermodynamic and kinetic binding parameters.•RESAn1 has a higher binding affinity toward HSA than does RES.•The RES-HSA and RESAn1-HSA complex formation was entropically driven.•Formation of the activated complex from the association was faster than dissociation.