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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| Main Authors: | , , , , , , |
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| Format: | Article |
| Language: | English |
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Wiley
2024-01-01
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| Series: | Journal of Spectroscopy |
| Online Access: | http://dx.doi.org/10.1155/2024/9923310 |
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| author | Xian-Kun Su Zhen-Chun Sun Chang-You Zhao Hui Yang Tian-Ming Zhao Chao Ma Guo-Fei Zhu |
| author_facet | Xian-Kun Su Zhen-Chun Sun Chang-You Zhao Hui Yang Tian-Ming Zhao Chao Ma Guo-Fei Zhu |
| author_sort | Xian-Kun Su |
| collection | DOAJ |
| description | 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 < 0), with van der Waals interactions and hydrogen bonding as the primary driving forces (ΔH = −9.40 kJmol−1 and ΔS = −14.50 Jmol−1·K−1). The binding of α-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 α-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 α-cembrenediol and HSA, contributing to an improved understanding of the compound’s pharmacokinetic properties. |
| format | Article |
| id | doaj-art-644046a687c04832a814dfdc86d31e2c |
| institution | Kabale University |
| issn | 2314-4939 |
| language | English |
| publishDate | 2024-01-01 |
| publisher | Wiley |
| record_format | Article |
| series | Journal of Spectroscopy |
| spelling | doaj-art-644046a687c04832a814dfdc86d31e2c2025-02-03T01:29:25ZengWileyJournal of Spectroscopy2314-49392024-01-01202410.1155/2024/9923310Interaction of α-Cembrenediol with Human Serum Albumin Based on Spectroscopic and Computational AnalysesXian-Kun Su0Zhen-Chun Sun1Chang-You Zhao2Hui Yang3Tian-Ming Zhao4Chao Ma5Guo-Fei Zhu6Guizhou Academy of Tobacco ScienceGuizhou Academy of Tobacco ScienceGuizhou Institute of TechnologyGuizhou Academy of Tobacco ScienceGuizhou Institute of TechnologyGuizhou Institute of TechnologyGuizhou Institute of Technologyα-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 < 0), with van der Waals interactions and hydrogen bonding as the primary driving forces (ΔH = −9.40 kJmol−1 and ΔS = −14.50 Jmol−1·K−1). The binding of α-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 α-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 α-cembrenediol and HSA, contributing to an improved understanding of the compound’s pharmacokinetic properties.http://dx.doi.org/10.1155/2024/9923310 |
| spellingShingle | Xian-Kun Su Zhen-Chun Sun Chang-You Zhao Hui Yang Tian-Ming Zhao Chao Ma Guo-Fei Zhu Interaction of α-Cembrenediol with Human Serum Albumin Based on Spectroscopic and Computational Analyses Journal of Spectroscopy |
| title | Interaction of α-Cembrenediol with Human Serum Albumin Based on Spectroscopic and Computational Analyses |
| title_full | Interaction of α-Cembrenediol with Human Serum Albumin Based on Spectroscopic and Computational Analyses |
| title_fullStr | Interaction of α-Cembrenediol with Human Serum Albumin Based on Spectroscopic and Computational Analyses |
| title_full_unstemmed | Interaction of α-Cembrenediol with Human Serum Albumin Based on Spectroscopic and Computational Analyses |
| title_short | Interaction of α-Cembrenediol with Human Serum Albumin Based on Spectroscopic and Computational Analyses |
| title_sort | interaction of α cembrenediol with human serum albumin based on spectroscopic and computational analyses |
| url | http://dx.doi.org/10.1155/2024/9923310 |
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