文献类型：期刊文献

英文题名：Interaction of α-Cembrenediol with Human Serum Albumin Based on Spectroscopic and Computational Analyses

作者：Su, Xian-Kun Sun, Zhen-Chun Zhao, Chang-You Yang, Hui Zhao, Tian-Ming Ma, Chao Zhu, Guo-Fei

第一作者：Su, Xian-Kun

通信作者：Zhu, GF[1]

机构：[1]Guizhou Acad Tobacco Sci, Guiyang 550081, Peoples R China;[2]Guizhou Inst Technol, Sch Food & Drug Mfg Engn, Guiyang 550003, Peoples R China

第一机构：Guizhou Acad Tobacco Sci, Guiyang 550081, Peoples R China

通信机构：corresponding author), Guizhou Inst Technol, Sch Food & Drug Mfg Engn, Guiyang 550003, Peoples R China.|贵州理工学院;

年份：2024

卷号：2024

外文期刊名：JOURNAL OF SPECTROSCOPY

收录：;WOS:【SCI-EXPANDED(收录号:WOS:001259416800001)】；

基金：This work was supported by the China Tobacco Guizhou Industrial Corporation Science and Technology Project (2021XM25) and the Science and Technology Plan Project of Guizhou Province (No. [2020]4102, Qiankehe Platform Talent). Their support was instrumental in the completion of this research.

语种：英文

摘要：alpha-Cembrenediol exhibits a wide range of biological activities, including antibacterial, antitumor, and neuroprotective effects. However, knowledge of the absorption, transport, and release of alpha-cembrenediol in drug metabolism within the body is currently limited. Therefore, we aimed to gain a comprehensive understanding of the in vivo transport, distribution, and elimination mechanisms of alpha-cembrenediol and investigate the interaction between alpha-cembrenediol and HSA. To this end, we utilized various methods including UV absorption spectroscopy, steady-state fluorescence analysis, circular dichroism measurements, molecular docking studies, and molecular dynamics simulations. The results of the UV and fluorescence spectra clearly demonstrated that HSA interacts with alpha-cembrenediol. Specifically, the fluorescence spectra results showed that at a temperature of 310 K, the fluorescence quenching constant (K-SV) and binding constant (K-b) between HSA and alpha-cembrenediol were determined to be 1.28 x 10(3) Lmol(-1) and 218.27 Lmol(-1), respectively. As the temperature was decreased from 310 K to 293 K, both K-SV and K-b values increased, indicating the presence of a static quenching mechanism throughout the interaction process. Moreover, the results indicated the presence of a singular, specific binding site for alpha-cembrenediol on HSA, as evidenced by an approximate count of one binding site at all three temperatures. Additionally, this binding process occurred spontaneously (Delta G < 0), with van der Waals interactions and hydrogen bonding as the primary driving forces (Delta H = -9.40 kJmol(-1) and Delta S = -14.50 Jmol(-1)K-1). The binding of alpha-cembrenediol to Sudlow site I of HSA was confirmed through molecular docking, a combination of fluorescence probe substitution, and molecular dynamics simulation experiments. Moreover, the results demonstrated that alpha-cembrenediol binding led to alterations in the structural conformation of HSA, as confirmed by three-dimensional fluorescence, synchronous fluorescence, and circular dichroism spectra. This study offers crucial insights into the interaction between alpha-cembrenediol and HSA, contributing to an improved understanding of the compound's pharmacokinetic properties.