Binding of Puerarin to Human Serum Albumin: A Spectroscopic Analysis and Molecular Docking

Abstract

Puerarin is a widely used compound in Chinese traditional medicine and exhibits many pharmacological activities. Binding of puerarin to human serum albumin (HSA) was investigated by ultraviolet absorbance, fluorescence, circular dichroism and molecular docking. Puerarin caused a static quenching of intrinsic fluorescence of HSA, the quenching data was analyzed by Stern-Volmer equation. There was one primary puerarin binding site on HSA with a binding constant of 4.12 x 10(4) M(-1) at 298 K. Thermodynamic analysis by Van Hoff equation found enthalpy change (DeltaH(0)) and entropy change (DeltaS(0)) were -28.01 kJ/mol and -5.63 J/mol K respectively, which indicated the hydrogen bond and Van der Waas interaction were the predominant forces in the binding process. Competitive experiments showed a displacement of warfarin by puerarin, which revealed that the binding site was located at the drug site I. Puerarin was about 2.22 nm far from the tryptophan according to the observed fluorescence resonance energy transfer between HSA and puerarin. Molecular docking suggested the hydrophobic residues such as tyrosine (Tyr) 150, Tyr 148, Tyr 149 and polar residues such as lysine (Lys) 199, Lys 195, arginine 257 and histidine 242 played an important role in the binding reaction.

Design, synthesis and biological evaluation of berberine-benzimidazole hybrids as new type of potentially DNA-targeting antimicrobial agents

“…[35,36]. In this study molecular docking simulation has been used to improve the understanding of the interaction of drug to HSA [37][38][39]. As shown in the Figure 11 …”

One-Pot Multicomponent Synthesis of Thiourea Derivatives in Cyclotriphosphazenes Moieties

“…The bonding provides specificity and stabilisation of binding between a and enzyme active site which consequently enhanced the binding affinity [38,39]. Other basic residues such as Pro 1154, Ile 1153, Val 1213, Ala 1254, Hoh 2087, Hoh 2067, Arg 171, and Gly 242 were observed in the vicinity of compound a, which suggested that a strong electrostatic interaction was also involved in the binding process [40].…”

A Study of the Interaction Betweentrans-Dehydrocrotonin, a Bioactive Natural 19-nor-Clerodane, and Serum Albumin

“…45 CD spectra of BSA exhibited two negative bands at 208 and 222 nm, characteristic of α-helix structure units of the protein. 46 CD spectra (200-260 nm) of BSA were recorded in the absence and presence, at different concentrations, of t-DCTN at 296, 303 and 310 K ( Figure 5). Upon increasing the t-DCTN concentration in the albumin solution, a small and a moderate decrease in the intensity at 208 and 222 nm, respectively, can be clearly observed.…”