Investigation on the differences of four flavonoids with similar structure binding to human serum albumin

Abstract

Flavonoids are structurally diverse and the most ubiquitous groups of polyphenols distributed in the various plants, which possess intensive biological activities. In this study, the interaction mechanisms between four flavonoids containing one glucose unit with similar molecular weight isolated from the Tibetan medicinal herb Pyrethrum tatsienense, namely, apigenin-7-O-β-D-glucoside(1), luteolin-7-O-β-D-glucoside(2), quercetin-7-O-β-D-glucoside(3), quercetin-3-O-β-D-glycoside(4), and human serum albumin(HSA), were investigated by fluorescence, UV–vis absorbance, circular dichroism, and molecular modeling. The effects of biological metal ions Mg2+, Zn2+, and Cu2+ on the binding affinity between flavonoids and HSA were further examined. Structure–activity relationships of four flavonoids binding to HSA were discussed in depth and some meaningful conclusions have been drawn by the experiment data and theoretical simulation. In addition, an interesting phenomenon was observed that the microenvironment of the binding site I in HSA has hardly changed in the presence of 4 differentiating from the other three flavonoids on the basis of conformation investigations.

Interaction of repaglinide with bovine serum albumin: Spectroscopic and molecular docking approaches

“…So, more amount of RPG is freely released which is available to the targeted tissues as compared to RPG released from plasma. This facilitates the RPG to deliver its optimum medicinal effects [12,45].…”

“…Fluorescence emission spectra of RPG-BSA system were recorded at 298 K in the presence and absence of Cu 2+ and Zn 2+ ions, separately. For this, the concentration of BSA and metal ion was kept constant (1.67 μM) whereas that of RPG was varied from 1.67 to 15.0 μM [11,12].…”

Flavonoids-Macromolecules Interactions in Human Diseases with Focus on Alzheimer, Atherosclerosis and Cancer

“…Several studies have been performed to characterize the interactions between dietary flavonoids and proteins, mainly serum and food-related proteins, for example, serum albumins and β-casein [ 26 , 27 , 28 , 29 , 30 ]. Flavonoid–protein interactions mainly occur by noncovalent bonding that is derived from hydrophobic, van der Waals, hydrogen bridge-binding, and ionic interactions, which can change protein conformations and enzyme activities [ 31 ].…”

Double-Site Binding and Anti-/Pro-oxidation of Luteolin on Bovine Serum Albumin Mediated by Copper(II) Coordination

“…Docking of Lut and Cu(II) Binding with BSA. Site 1 in subdomain IIA for Lut according to the results in sitespecific experiments and the literature 17,32 and the Asp-Thr-His triad in the N-terminal for Cu(II), 33 the two binding sites in BSA, were set as the molecular docking center for Lut and Cu(II), respectively, by using the Autodock 4.2.6 software package. 28 The same crystal structure of BSA as in MD was given as a receptor for molecular docking.…”