Characterization of thymoquinone binding to human α₁-acid glycoprotein.

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.

journal_name

J Pharm Sci

authors

Lupidi G,Camaioni E,Khalifé H,Avenali L,Damiani E,Tanfani F,Scirè A

doi

10.1002/jps.23138

subject

Has Abstract

pub_date

2012-07-01 00:00:00

pages

2564-73

issue

7

eissn

0022-3549

issn

1520-6017

pii

S0022-3549(15)31523-9

journal_volume

101

pub_type

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