Abstract
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.
Highlights
Human serum albumin (HSA), the most abundant protein in plasma, is constituted by a single chain of 585 residues arranged in a globular heart-shaped conformation (Figure 1)containing three homologous domains usually indicated as I, II, and III
This study investigates the effects of the ALK (caffeine (CAF)) and FLAVs (catechin (CAT), quercetin (QUE) and diosmin (DIO)) (Figure 2) on binding tigecycline (TGC) to HSA, as well as their effects on the structure of the active site and the nature of interactions, in order to find out how food that is rich in these compounds can affect the use of TGC
We observed the change in the UV–Vis absorption spectra of the HSATGC-CAF/FLAV (QUE, CAT and DIO) system in the presence of varying concentrations of TGC
Summary
Containing three homologous domains usually indicated as I, II, and III. Each domain includes two separate subdomains (A and B) [1]. HSA has the capability of binding reversibly to a large variety of drugs via its binding sites. Crystal structure analysis indicates that hydrophobic cavities in subdomains IIA and IIIA in albumin are the principal regions of ligand binding sites for aromatic and heterocyclic drugs [2,3]. It is of great importance from the viewpoint of pharmaceutical sciences to clarify the structure, function, and properties of HSA–drug complexes.
Sign-in/Register to view highlights & summary Sign-in/Register to access full text options 
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a callDisclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.
