Research on the Interaction Mechanism and Structural Changes in Human Serum Albumin with Hispidin Using Spectroscopy and Molecular Docking
The interaction between human serum albumin (HSA) and hispidin, a polyketide abundantly present in both edible and therapeutic mushrooms, was explored through multispectral methods, hydrophobic probe assays, location competition trials, and molecular docking simulations. The results of fluorescence...
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MDPI AG
2024-01-01
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| Series: | Molecules |
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| Online Access: | https://www.mdpi.com/1420-3049/29/3/655 |
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| author | Si-Hua Fan Wen-Qiang Wang Yu-Wen Zhou Xue-Jun Gao Qiang Zhang Ming-Hui Zhang |
| author_facet | Si-Hua Fan Wen-Qiang Wang Yu-Wen Zhou Xue-Jun Gao Qiang Zhang Ming-Hui Zhang |
| author_sort | Si-Hua Fan |
| collection | DOAJ |
| description | The interaction between human serum albumin (HSA) and hispidin, a polyketide abundantly present in both edible and therapeutic mushrooms, was explored through multispectral methods, hydrophobic probe assays, location competition trials, and molecular docking simulations. The results of fluorescence quenching analysis showed that hispidin quenched the fluorescence of HSA by binding to it via a static mechanism. The binding of hispidin and HSA was validated further by synchronous fluorescence, three-dimensional fluorescence, and UV/vis spectroscopy analysis. The apparent binding constant (Ka) at different temperatures, the binding site number (n), the quenching constants (Ksv), the dimolecular quenching rate constants (Kq), and the thermodynamic parameters (∆G, ∆H, and ∆S) were calculated. Among these parameters, ∆H and ∆S were determined to be 98.75 kJ/mol and 426.29 J/(mol·K), respectively, both exhibiting positive values. This observation suggested a predominant contribution of hydrophobic forces in the interaction between hispidin and HSA. By employing detergents (SDS and urea) and hydrophobic probes (ANS), it became feasible to quantify alterations in Ka and surface hydrophobicity, respectively. These measurements confirmed the pivotal role of hydrophobic forces in steering the interaction between hispidin and HSA. Site competition experiments showed that there was an interaction between hispidin and HSA molecules at site I, which situates the IIA domains of HSA, which was further confirmed by the molecular docking simulation. |
| first_indexed | 2024-03-08T03:52:07Z |
| format | Article |
| id | doaj.art-c4de14b097f24504a4e599cc1148e726 |
| institution | Directory Open Access Journal |
| issn | 1420-3049 |
| language | English |
| last_indexed | 2024-03-08T03:52:07Z |
| publishDate | 2024-01-01 |
| publisher | MDPI AG |
| record_format | Article |
| series | Molecules |
| spelling | doaj.art-c4de14b097f24504a4e599cc1148e7262024-02-09T15:18:59ZengMDPI AGMolecules1420-30492024-01-0129365510.3390/molecules29030655Research on the Interaction Mechanism and Structural Changes in Human Serum Albumin with Hispidin Using Spectroscopy and Molecular DockingSi-Hua Fan0Wen-Qiang Wang1Yu-Wen Zhou2Xue-Jun Gao3Qiang Zhang4Ming-Hui Zhang5College of Biology and Food Engineering, Guangdong University of Petrochemical Technology, No. 1, Kechuang Road, Maonan District, Maoming 525000, ChinaCollege of Biology and Food Engineering, Guangdong University of Petrochemical Technology, No. 1, Kechuang Road, Maonan District, Maoming 525000, ChinaCollege of Animal Science and Technology, Yangtze University, 88 Jingmi Road, Jingzhou District, Jingzhou 434025, ChinaCollege of Animal Science and Technology, Yangtze University, 88 Jingmi Road, Jingzhou District, Jingzhou 434025, ChinaCollege of Biology and Food Engineering, Guangdong University of Petrochemical Technology, No. 1, Kechuang Road, Maonan District, Maoming 525000, ChinaCollege of Animal Science and Technology, Yangtze University, 88 Jingmi Road, Jingzhou District, Jingzhou 434025, ChinaThe interaction between human serum albumin (HSA) and hispidin, a polyketide abundantly present in both edible and therapeutic mushrooms, was explored through multispectral methods, hydrophobic probe assays, location competition trials, and molecular docking simulations. The results of fluorescence quenching analysis showed that hispidin quenched the fluorescence of HSA by binding to it via a static mechanism. The binding of hispidin and HSA was validated further by synchronous fluorescence, three-dimensional fluorescence, and UV/vis spectroscopy analysis. The apparent binding constant (Ka) at different temperatures, the binding site number (n), the quenching constants (Ksv), the dimolecular quenching rate constants (Kq), and the thermodynamic parameters (∆G, ∆H, and ∆S) were calculated. Among these parameters, ∆H and ∆S were determined to be 98.75 kJ/mol and 426.29 J/(mol·K), respectively, both exhibiting positive values. This observation suggested a predominant contribution of hydrophobic forces in the interaction between hispidin and HSA. By employing detergents (SDS and urea) and hydrophobic probes (ANS), it became feasible to quantify alterations in Ka and surface hydrophobicity, respectively. These measurements confirmed the pivotal role of hydrophobic forces in steering the interaction between hispidin and HSA. Site competition experiments showed that there was an interaction between hispidin and HSA molecules at site I, which situates the IIA domains of HSA, which was further confirmed by the molecular docking simulation.https://www.mdpi.com/1420-3049/29/3/655human serum albuminhispidinfluorescence surveymolecular dockingspectrophotometry |
| spellingShingle | Si-Hua Fan Wen-Qiang Wang Yu-Wen Zhou Xue-Jun Gao Qiang Zhang Ming-Hui Zhang Research on the Interaction Mechanism and Structural Changes in Human Serum Albumin with Hispidin Using Spectroscopy and Molecular Docking Molecules human serum albumin hispidin fluorescence survey molecular docking spectrophotometry |
| title | Research on the Interaction Mechanism and Structural Changes in Human Serum Albumin with Hispidin Using Spectroscopy and Molecular Docking |
| title_full | Research on the Interaction Mechanism and Structural Changes in Human Serum Albumin with Hispidin Using Spectroscopy and Molecular Docking |
| title_fullStr | Research on the Interaction Mechanism and Structural Changes in Human Serum Albumin with Hispidin Using Spectroscopy and Molecular Docking |
| title_full_unstemmed | Research on the Interaction Mechanism and Structural Changes in Human Serum Albumin with Hispidin Using Spectroscopy and Molecular Docking |
| title_short | Research on the Interaction Mechanism and Structural Changes in Human Serum Albumin with Hispidin Using Spectroscopy and Molecular Docking |
| title_sort | research on the interaction mechanism and structural changes in human serum albumin with hispidin using spectroscopy and molecular docking |
| topic | human serum albumin hispidin fluorescence survey molecular docking spectrophotometry |
| url | https://www.mdpi.com/1420-3049/29/3/655 |
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