Interaction of α-Cembrenediol with Human Serum Albumin Based on Spectroscopic and Computational Analyses

α-Cembrenediol exhibits a wide range of biological activities, including antibacterial, antitumor, and neuroprotective effects. However, knowledge of the absorption, transport, and release of α-cembrenediol in drug metabolism within the body is currently limited. Therefore, we aimed to gain a compre...

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Bibliographic Details
Published in:Journal of spectroscopy (Hindawi) 2024-01, Vol.2024
Main Authors: Xian-Kun Su, Zhen-Chun, Sun, Chang-You, Zhao, Yang, Hui, Tian-Ming, Zhao, Ma, Chao, Guo-Fei, Zhu
Format: Article
Language:English
Subjects:
Absorption spectroscopy
Anticancer properties
Binding sites
Dichroism
Fluorescent indicators
Hydrogen bonding
In vivo methods and tests
Ligands
Molecular docking
Molecular dynamics
Nonsteroidal anti-inflammatory drugs
Physiology
Proteins
Quenching
Serum albumin
Simulation
Spectra
Spectrum analysis
Temperature
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Summary:α-Cembrenediol exhibits a wide range of biological activities, including antibacterial, antitumor, and neuroprotective effects. However, knowledge of the absorption, transport, and release of α-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 α-cembrenediol and investigate the interaction between α-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 α-cembrenediol. Specifically, the fluorescence spectra results showed that at a temperature of 310 K, the fluorescence quenching constant (KSV) and binding constant (Kb) between HSA and α-cembrenediol were determined to be 1.28 × 103 Lmol−1 and 218.27 Lmol−1, respectively. As the temperature was decreased from 310 K to 293 K, both KSV and Kb 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 α-cembrenediol on HSA, as evidenced by an approximate count of one binding site at all three temperatures. Additionally, this binding process occurred spontaneously (ΔG 
ISSN:2314-4920
2314-4939
DOI:10.1155/2024/9923310