Indomethacin increases quercetin affinity for human serum albumin: a combined experimental and computational study and its broader implications (CROSBI ID 281867)
Prilog u časopisu | izvorni znanstveni rad | međunarodna recenzija
Podaci o odgovornosti
Rimac, Hrvoje ; Tandarić, Tana ; Vianello, Robert ; Bojić, Mirza
engleski
Indomethacin increases quercetin affinity for human serum albumin: a combined experimental and computational study and its broader implications
Human serum albumin (HSA) is the most abundant carrier protein in human body. Competition for the same binding site between different ligands can lead to an increased active concentration or a faster elimination of one or both ligands. Indomethacin and quercetin both bind to the binding site located in the IIA subdomain. To determine the nature of HSA-indomethacin- quercetin interactions, spectrofluorometric, docking, molecular dynamics studies, and quantum chemical calculations were performed. Results show that indomethacin and quercetin binding sites do not overlap. Moreover, the presence of quercetin does not influence the binding constant and position of indomethacin in the pocket. However, binding of quercetin is much more favorable in the presence of indomethacin, with its position and interactions with HSA significantly changed. These results provide a new insight into drug-drug interactions, which can be important in situations when displacement from HSA or other proteins is undesirable or even desirable. This principle could also be used to deliberately prolong or shorten xenobiotics’ half-life in the body, depending on the desired outcomes.
human serum albumin ; quercetin ; indomethacin ; pharmacokinetic interactions ; fluorescence spectroscopy ; docking ; molecular dynamics ; quantum chemistry
nije evidentirano
nije evidentirano
nije evidentirano
nije evidentirano
nije evidentirano
nije evidentirano
Podaci o izdanju
21 (16)
2020.
5740
14
objavljeno
1422-0067
10.3390/ijms21165740