Binding Studies Between Dinotefuran and Bovine Serum Albumin Using Multiple Analytical Approaches

Abstract

The present study examines the interaction between bovine serum albumin (BSA) and dinotefuran utilizing spectroscopic, electrochemical, and computational approaches. The examination of fluorescence spectroscopy demonstrates the formation of a stable complex (protein-ligand) between dinotefuran and BSA, with a binding coefficient of 3.8 × 108 M−1 and a stoichiometry of 2:1 (dinotefuran to BSA). The presence of static quenching phenomena indicates the creation of a non-covalent compound. UV spectroscopy and circular dichroism spectroscopy confirm the development of the dinotefuran-BSA complex. Molecular docking simulations reveal the interaction between dinotefuran and specific amino acid residues of BSA with a binding energy (B.E.) of −5.4 kcal mol−1. The stability of the dinotefuran-BSA complex is confirmed using molecular dynamics simulations, as evidenced by extracted trajectories. Electrochemical investigations reveal a slow and continuous interaction between dinotefuran and BSA, as indicated by the steady reduction in the intensity of the dinotefuran peak over time. This thorough examination offers unique insights into the molecular interactions between dinotefuran and BSA, providing new perspectives on their binding mechanisms and implications in biological systems.