Calorimetric and spectroscopic studies on the competitive behavior between (−)-epigallocatechin-3-gallate and 5-fluorouracil with human serum albumin
作者： Lixia Yuan , Min Liu , Bin Sun , Jie Liu , Xilian Wei
DOI: 10.1016/J.MOLLIQ.2017.10.049
关键词: Hydrogen bond 、 Hydrophobic effect 、 Isothermal titration calorimetry 、 Stereochemistry 、 Human serum albumin 、 van der Waals force 、 Binding site 、 Biophysics 、 Dynamic light scattering 、 Circular dichroism 、 Chemistry
摘要: Abstract The combination of several drugs is often necessary, especially during long-term therapy. Drug-protein interaction has attracted a great deal research interest because only the free drug fraction exerts pharmacological and/or toxicological effects. Herein, binding interactions serum transport protein, human albumin (HSA), with individual or combined anticancer drugs, (−)-epigallocatechin-3-gallate (EGCG) and 5-fluorouracil (FU), were investigated using isothermal titration calorimetry (ITC), circular dichroism (CD), dynamic light scattering (DLS). DLS measurements showed that EGCG larger effect on hydrodynamic diameter HSA than FU. adding order FU an important influence size EGCG + FU + HSA complex. Fitting ITC data suggested there are two sets sites for to HSA. obtained thermodynamic parameters revealed electrostatic, hydrogen bonding, van der Waals may contribute stronger affinity while hydrophobic interactions, forces, bonding major forces in stabilizing FU + HSA largest concentrations attained at pH 7.4 8.4 respectively, due pH dependence number constants. discrepancy concentration between binary ternary systems implies competitive Changes secondary structure addition different pHs discussed based CD measurements. calorimetric spectroscopic results can provide quantitative information characteristics suggest enhance These deeper understanding
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