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.
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