期刊
INTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULES
卷 165, 期 -, 页码 2451-2461出版社
ELSEVIER
DOI: 10.1016/j.ijbiomac.2020.10.098
关键词
Sorafenib; Human serum albumin; Fluorescence quenching; Binding interaction; Quercetin; Rutin
资金
- Ministry of Education in Saudi Arabia [IFKSURG-1435-073]
The main mechanism for drug-drug interaction is displacement reaction of ligands from their protein binding sites. The aim of this study was to evaluate anticancer drug sorafenib displacement from the binding site on human serum albumin by commonly used plant flavonoids quercetin and rutin. The interaction between biomacromolecules and drugs can also cause changes in protein structure and therefore was evaluated in this study by spectroscopic and molecular dynamic simulation techniques. Serum albumin, the main protein in the plasma acts in the disposition of many drugs and therefore, is a model protein for investigating drug/ligand binding and alteration in the spectrophotometric and molecular docking properties of drug/ligand. All the studied ligands sorafenib, quercetin and rutin bind to HSA with different binding affinity. The displacement of ligands from their binding sites was inferred from comparison of quenching and binding constants of binary and ternary systems. Conformational changes in the HSA were found with UV-spectroscopic, circular dichroism, FT-IR and three dimensional studies. The molecular dynamic simulation studies suggest a stable complex formation between HSA and sorafenib. Binding studies for HSA-sorafenib in presence of quercetin and rutin indicated displacement of sorafenib from its binding site. (C) 2020 Elsevier B.V. All rights reserved.
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