Catechol derivatives interact with bovine serum albumin: Correlation of non-covalent interactions and antioxidant activity

Abstract

The interactions of catechol derivatives with model transportation protein-bovine serum albumin (BSA) were deciphered by the multispectral techniques, molecular docking and multifunctional wavefunction (Multiwfn). The representative catechol derivatives caffeic acid (CA) and 1-monocaffeoyl glycerol (1-MCG) with an (E)-but-2-enoic acid and a 2,3-dihydroxypropyl(E)-but-2-enoate side chain, respectively, were chosen in present study. The interaction results revealed the extra non-polar interactions and abundant binding sites facilitate the easier and stronger binding of 1-MCG-BSA. The α-helix content of BSA decreased and the hydrophilicity around Tyr and Trp changed due to the different interaction between catechol and BSA. The H2O2-damaged RAW 264.7, HaCat and SH-SY5Y were applied to investigate the anti-ROS properties of the catechol-BSA complexes. The results illuminated that the 2,3-dihydroxypropyl(E)-but-2-enoate side chain of 1-MCG facilitated the preferable biocompatibility and antioxidant property of its binding complex. These results revealed that the interaction of catechol-BSA binding complexes could influence their biocompatibility and antioxidant properties.