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Probing the Interaction between Human Serum Albumin and 9-Hydroxyphenanthrene: A Spectroscopic and Molecular Docking Study.

ABSTRACT: 9-Hydroxyphenanthrene (9-OHPhe), the representative hydroxyl metabolite of phenanthrene, has generated increasing concern as it is potentially hazardous to organisms. Herein, multispectroscopic and molecular docking techniques were applied to investigate the molecular interaction of human serum albumin (HSA) with 9-hydroxyphenanthrene (9-OHPhe) under simulated physiological conditions. Steady-state fluorescence and time-resolved fluorescence spectral analysis showed that 9-OHPhe quenched HSA fluorescence through a mixed static and dynamic process. HSA can bind with 9-OHPhe to form a 1:1 complex, with binding constants of 1.28 × 105, 1.36 × 105, and 1.26 × 105 L·mol-1 at 298.15, 303.15, and 308.15 K, respectively. The strong binding between HSA and 9-OHPhe is spontaneous and entropy-driven. Molecular docking indicated that the optimal binding site of 9-OHPhe with HSA was located in the IA subdomain of HSA. Thermodynamic analysis and molecular docking results suggested that hydrophobic interactions and hydrogen bond force dominated the binding process of HSA with 9-OHPhe. Specifically, 9-OHPhe formed hydrophobic interactions with LEU134, LEU139, ILE142, LEU154, PHE157, ALA158, and TYR161 and formed a 1.86 Å hydrogen bond with LEU135. Circular dichroism spectral analysis showed that the ?-helical content of HSA decreased from 52.3 to 50.9% after adding 9-OHPhe with a ratio of 1:1. The obtained results are hoped to provide basic data for understanding the potential effects of the hydroxyl metabolites of PAHs on functional biomacromolecules.

SUBMITTER: Zhang J

PROVIDER: S-EPMC7364716 | biostudies-literature | 2020 Jul

REPOSITORIES: biostudies-literature

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Probing the Interaction between Human Serum Albumin and 9-Hydroxyphenanthrene: A Spectroscopic and Molecular Docking Study.

Zhang Jing J Gao Xuan X Huang Jinyang J Wang Honghui H

ACS omega 20200703 27

9-Hydroxyphenanthrene (9-OHPhe), the representative hydroxyl metabolite of phenanthrene, has generated increasing concern as it is potentially hazardous to organisms. Herein, multispectroscopic and molecular docking techniques were applied to investigate the molecular interaction of human serum albumin (HSA) with 9-hydroxyphenanthrene (9-OHPhe) under simulated physiological conditions. Steady-state fluorescence and time-resolved fluorescence spectral analysis showed that 9-OHPhe quenched HSA flu ...[more]

PMID: 32685852

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Project description:BackgroundBovine serum albumin (BSA) contains high affinity binding sites for several endogenous and exogenous compounds and has been used to replace human serum albumin (HSA), as these two compounds share a similar structure. Naringin palmitate is a modified product of naringin that is produced by an acylation reaction with palmitic acid, which is considered to be an effective substance for enhancing naringin lipophilicity. In this study, the interaction of naringin palmitate with BSA was characterised by spectroscopic and molecular docking techniques.Methodology/principal findingsThe goal of this study was to investigate the interactions between naringin palmitate and BSA under physiological conditions, and differences in naringin and naringin palmitate affinities for BSA were further compared and analysed. The formation of naringin palmitate-BSA was revealed by fluorescence quenching, and the Stern-Volmer quenching constant (KSV ) was found to decrease with increasing temperature, suggesting that a static quenching mechanism was involved. The changes in enthalpy (?H) and entropy (?S) for the interaction were detected at -4.11 ± 0.18 kJ·mol(-1) and -76.59 ± 0.32 J·mol(-1)·K(-1), respectively, which indicated that the naringin palmitate-BSA interaction occurred mainly through van der Waals forces and hydrogen bond formation. The negative free energy change (?G) values of naringin palmitate at different temperatures suggested a spontaneous interaction. Circular dichroism studies revealed that the ?-helical content of BSA decreased after interacting with naringin palmitate. Displacement studies suggested that naringin palmitate was partially bound to site I (subdomain IIA) of the BSA, which was also substantiated by the molecular docking studies.Conclusions/significanceIn conclusion, naringin palmitate was transported by BSA and was easily removed afterwards. As a consequence, an extension of naringin applications for use in food, cosmetic and medicinal preparations may be clinically and practically significant, especially in the design of new naringin palmitate-inspired drugs.

Dataset Information

Probing the Interaction between Human Serum Albumin and 9-Hydroxyphenanthrene: A Spectroscopic and Molecular Docking Study.

Publications

Probing the Interaction between Human Serum Albumin and 9-Hydroxyphenanthrene: A Spectroscopic and Molecular Docking Study.

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