Multispectroscopic and Computational Study of the Interaction between α-Cembrenediol and Bovine Serum Albumin

Abstract

α-Cembrenediol displays a diverse array of biological activities, encompassing antibacterial, antitumor, and neuroprotective effects. To comprehensively understand the in vivo transport, distribution, and elimination mechanisms associated with α-cembrenediol, its interaction with bovine serum albumin (BSA) was investigated. In this study, the interaction between α-cembrenediol and BSA was explored using various techniques, including UV absorption, steady-state fluorescence, circular dichroism spectrum, molecular docking, and molecular dynamics simulation. The results showed that there was a clear interaction between BSA and α-cembrenediol. Specifically, the KSV and Kb decreased with increasing temperature at 293, 303, and 310 K, indicating that α-cembrenediol interacted with BSA through a static quenching mechanism. Furthermore, the number of binding sites was approximately 1 at the three temperatures, suggesting the presence of a single specific binding site for α-cembrenediol on BSA. Moreover, the binding process occurred spontaneously (ΔG<0), primarily driven by hydrogen bonds and van der Waals forces (ΔH<0 and ΔS<0). α-Cembrenediol bound to the Sudlow site I of BSA. Binding of BSA to α-cembrenediol also caused its conformation to change. This study provides essential insights into the interaction between α-cembrenediol and BSA, contributing to a better understanding of the pharmacokinetic properties of the compound.

Keywords

• α-cembrenediol
• bovine serum albumin
• interaction
• fluorescence spectroscopy
• molecular docking