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Study on the interaction of paeoniflorin with human serum albumin (HSA) by spectroscopic and molecular docking techniques.

ABSTRACT: The interaction of paeoniflorin with human serum albumin (HSA) was investigated using fluorescence, UV-vis absorption, circular dichroism (CD) spectra and molecular docking techniques under simulative physiological conditions. The results clarified that the fluorescence quenching of HSA by paeoniflorin was a static quenching process and energy transfer as a result of a newly formed complex (1:1). Paeoniflorin spontaneously bound to HSA in site I (subdomain IIA), which was primarily driven by hydrophobic forces and hydrogen bonds (?H° = - 9.98 kJ mol-1, ?S° = 28.18 J mol-1 K-1). The binding constant was calculated to be 1.909 × 103 L mol-1 at 288 K and it decreased with the increase of the temperature. The binding distance was estimated to be 1.74 nm at 288 K, showing the occurrence of fluorescence energy transfer. The results of CD and three-dimensional fluorescence spectra showed that paeoniflorin induced the conformational changes of HSA. Meanwhile, the study of molecular docking also indicated that paeoniflorin could bind to the site I of HSA mainly by hydrophobic and hydrogen bond interactions.

SUBMITTER: Xu L

PROVIDER: S-EPMC5691829 | biostudies-literature | 2017 Nov

REPOSITORIES: biostudies-literature

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Study on the interaction of paeoniflorin with human serum albumin (HSA) by spectroscopic and molecular docking techniques.

Xu Liang L Hu Yan-Xi YX Li Yan-Cheng YC Liu Yu-Feng YF Zhang Li L Ai Hai-Xin HX Liu Hong-Sheng HS

Chemistry Central journal 20171117 1

The interaction of paeoniflorin with human serum albumin (HSA) was investigated using fluorescence, UV-vis absorption, circular dichroism (CD) spectra and molecular docking techniques under simulative physiological conditions. The results clarified that the fluorescence quenching of HSA by paeoniflorin was a static quenching process and energy transfer as a result of a newly formed complex (1:1). Paeoniflorin spontaneously bound to HSA in site I (subdomain IIA), which was primarily driven by hyd ...[more]

PMID: 29150749

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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

Study on the interaction of paeoniflorin with human serum albumin (HSA) by spectroscopic and molecular docking techniques.

Publications

Study on the interaction of paeoniflorin with human serum albumin (HSA) by spectroscopic and molecular docking techniques.

Similar Datasets

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