RESUMEN
Human serum albumin (HSA) has a very significant role in the transport of drugs, in their pharmacokinetic and pharmacodynamic properties, as well as the unbound concentration of drugs in circulating plasma. The aim of this study was to look into the competition between tigecycline (TGC) and alkaloid (ALK) (caffeine (CAF)), and flavonoids (FLAVs) (catechin (CAT), quercetin (QUE), and diosmin (DIO)) in binding to HSA in simulated physiological conditions using multiple spectroscopic measurements and docking simulations. Fluorescence analysis was used to find the binding and quenching properties of double HSA-TGC and triple HSA-TGC-CAF/FLAV systems. The conformational change of the HSA was analyzed using synchronous fluorescence spectroscopy, Fourier transform infrared spectroscopy, and circular dichroism. Obtained results of spectroscopic analyses indicate that triple complexes of HSA-TGC-CAF/FLAVs are formed without problems and have higher binding affinities than double HSA-TGC. In addition, TGC does not change the microenvironments around the tryptophan (Trp) and tyrosine (Tyr) residues in the presence of ALK and FLAVs. Ultimately, the binding affinity, competition, and interaction nature were explored by docking modeling. Computational outcomes are in good accordance with experimentally obtained results. Accordingly, concluding remarks may be very useful for potential interactions between common food components and drugs.
RESUMEN
In this study, the binding of olanzapine (OLZ) to human serum albumin (HSA) and the influence of metal ions (Ca2+, Mg2+, Cu2+, Zn2+, Fe3+), caffeine (CAF) and flavonoids (diosmin (DIO), catechin (CAT), quercetin (QUE)), on their affinity, was investigated by fluorescence spectroscopy and UV-vis absorption spectroscopy. Fluorescence experiments suggest that OLZ quench the fluorescence of HSA through the mixed quenching mechanism and non-radiation energy transferring as a result of the HSA-OLZ complex formation. OLZ spontaneously bind in the site I on HSA, and according to thermodynamic parameters, the reaction was spontaneous and mainly driven by hydrogen bonds and van der Waals interactions. The presence of Mn+ ions, CAF, DIO and CAT decreased binding affinity between OLZ and HSA which indicates that they could compete against OLZ in the site I. Contrary, in the presence of QUE the binding affinity of the HSA-OLZ system enhanced, which may be explained by conformational changes in HSA (non-competitive interference).