Exploring the interactions of some PAHs with bovine serum albumin: spectroscopic method and chemometric approaches

Polycyclic aromatic hydrocarbons (PAHs) have been listed by the International Agency for Research on Cancer (IARC) as possible carcinogens. Serum albumins serve as major transport proteins in the blood circulation system [1]. Thus, the study of binding affinity of a ligand to serum albumin determines its pharmacokinetic and pharmacodynamics behavior. The intrinsic fluorescence of bovine serum albumin (BSA) facilitated employing fluorescence spectroscopy as a selective and sensitive technique to explore the in vitro interactions between some PAHs and BSA. Therefore, the quenching mechanism, the quenching constant, the binding constant and the number of binding sites involved in the studied BSA-PAHs complex were clarified utilizing quenching study. Molecular docking, a computational tool, has been used to simulate the intermolecular interactions of a ligand with proteins, which visually disclose preferred binding mode of a ligand within active site of the protein at the molecular level [2]. Hence, experimental methods combined with molecular docking simulations provide comprehensive insight into complex interactions of small molecules with proteins. Attempts were made to reveal the specific binding sites and modes of some PAHs on BSA employing molecular docking simulation. The results of the present work should help predict the toxic effects of PAHs on organisms.