A mutispectroscopic study on the structure-affinity relationship of the interactions of bisphenol analogues with bovine serum albumin.

Bisphenol A (BPA) is a recognized endocrine-disrupting chemical (EDC), and its analogues also exert negative effects on health. The structure-affinity relationship between the structures of nine bisphenol (BP) analogues and the conformational changes of bovine serum albumin (BSA) was studied by various characterization methods and molecular docking. BPs including BPA and its analogues, bisphenol B (BPB), bisphenol C (BPC), bisphenol AP (BPAP), bisphenol M (BPM), bisphenol P (BPP), bisphenol Z (BPZ), diethylstilbestrol (DES) and dienestrol (DS) interacted with BSA. At the concentration of 3.85 × 10-5 mol l-1, DS was found to lead to 64% quenching, while BPAP, BPM and DES quenched 60%, 59% and 55% of BSA fluorescence, respectively. The values of ΔH (-19.31-135.42 kJ mol-1) and ΔS (12.52-495.63 J mol-1 K-1) indicated that hydrophobic interactions and hydrogen bonds played important roles in the binding process. The binding constants of DS (8.87 × 104 l mol-1), DES (3.05 × 104 l mol-1), BPAP (1.52 × 104 l mol-1), BPC (1.16 × 104 l mol-1) and BPM (1.10 × 104 l mol-1) to BSA were greater than that of BPA (1.18 × 103 l mol-1) to BSA, indicating that they may exert more negative effects than BPA. The molecular structure differences of these BPs partly affected their ability to bind to BSA. The binding constants of BPB/BPP to BSA were smaller due to the steric hindrance of ethyl and benzene ring. BPs with conjugated double bond structures (DS and DES) and benzene ring structures (BPM, BPP, BPAP) had a greater influence on the conformation of BSA.