Exploring the interactions of acenaphthene with bovine serum albumin: Spectroscopic methods, molecular modeling and chemometric approaches

The interaction of acenaphthene (ACN), a widespread environmental pollutant, with bovine serum albumin (BSA) was explored using spectroscopic methods, molecular modeling and chemometric approaches. The multivariate curve resolution-alternating least squares (MCR-ALS) analysis decomposed the overlapped excitation-emission matrix (EEM) spectra of mixture of ACN and BSA successfully and extracted spectral profiles of pure BSA, ACN and BSA-ACN complex. Based on fluorescence quenching analysis, ACN quenched the inherent fluorescence of BSA remarkably via a static mechanism. The obtained value of binding constant (K-b = 3.82 x 10(5) L mol(-1)) revealed a high binding affinity of ACN to BSA which facilitates its distribution by blood circulation system. Furthermore, the binding parameters values revealed that one binding site in BSA was involved in BSA-ACN complex. FT-IR, UV-Vis and CD spectra showed that the conformation of BSA was altered in presence of ACN slightly. Molecular docking simulation suggested that ACN was located in the IA region of BSA and the main interactions between ACN and BSA, are van der Waals forces. The obtained results provide some insight into interactions between ACN and serum albumins at the molecular level. (C) 2021 Published by Elsevier B.V.

Automated summary

The study investigated the interaction of acenaphthene (ACN), an environmental pollutant, with bovine serum albumin (BSA) through spectroscopic methods, molecular modeling, and chemometric approaches. The results showed that ACN quenched the fluorescence of BSA via a static mechanism and exhibited a high binding affinity to BSA, with one binding site involved in the BSA-ACN complex. Furthermore, molecular docking simulations suggested that ACN interacted with BSA mainly through van der Waals forces in the IA region of BSA.