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Characterization of Thymoquinone Binding to Human α1-Acid Glycoprotein

Characterization of Thymoquinone Binding to Human α1-Acid Glycoprotein

Authors :
Emidio Camaioni
Elisabetta Damiani
Hamal Khalifé
Fabio Tanfani
Giulio Lupidi
Andrea Scirè
Luca Avenali
Source :
Journal of Pharmaceutical Sciences. 101:2564-2573
Publication Year :
2012
Publisher :
Elsevier BV, 2012.

Abstract

Thymoquinone (TQ) is the main bioactive component isolated from Nigella sativa essential oil and seeds and has been used for the treatment of inflammations, liver disorders, arthritis, and is of great importance as a promising therapeutic drug for different diseases including cancer. This paper reports the first experimental evidence on binding of TQ to human α(1)-acid glycoprotein (AGP), an important drug-binding glycoprotein in human plasma, which affects pharmacokinetic properties of various therapeutic agents. The interaction of TQ with AGP has been characterized by Fourier transform infrared (FTIR) and fluorescence spectroscopy, as well as by molecular docking experiments. FTIR spectroscopy showed that the binding of TQ to AGP slightly increases its thermal stability and shifts the existence of a molten globule-like state observed in a previous study to higher temperature. The binding constants K(a); the number of binding sites n; and the corresponding thermodynamic parameters ΔG, ΔH, and ΔS at different temperatures were calculated through fluorescence spectroscopy. Fluorescence quenching experiments indicated that TQ binding involves hydrophobic interactions and to a lower extent hydrogen bonds, in agreement with molecular docking experiments. The data on binding ability of TQ to AGP represent basic information for the TQ pharmacokinetics such as drug metabolism and distribution in the body.

Details

ISSN :
00223549
Volume :
101
Database :
OpenAIRE
Journal :
Journal of Pharmaceutical Sciences
Accession number :
edsair.doi.dedup.....0f0535fbd006a7e1856ba5b1d889fa2a
Full Text :
https://doi.org/10.1002/jps.23138