Study of the interaction between monoammonium glycyrrhizinate and bovine serum albumin

Hu, Yanjun; Liu, Yi; Wang, Jiabo; Song-Sheng, Qu

doi:10.1016/j.jpba.2004.08.021

Cited by 601 publications

(217 citation statements)

References 20 publications

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“…In Fig. 3, the change of peak before and after the addition of HEA testifies to the formation of a new complex in combination with obvious enhancement of the absorbency intensity A (25,26). Therefore, the quenching of HSA fluorescence by HEA depended on the formation of the new HEA-HSA complex.…”

Section: Mechanism Of Binding and Binding Parametersmentioning

confidence: 90%

Investigation of interaction between human serum albumin and N⁶‐(2‐hydroxyethyl)‐adenosine by fluorescence spectroscopy and molecular modelling

et al. 2007

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The interaction between human serum albumin (HSA) and N(6)-(2-hydroxyethyl)-adenosine (HEA) was investigated using fluorescence spectroscopy in combination with UV absorption spectroscopy for the first time. The results of spectroscopic measurements suggested that the hydrophobic interaction was the predominant intermolecular force stabilizing the complex, which was in good agreement with the results of molecular modelling study. The enthalpy change (DeltaH) and the entropy change (DeltaS) were calculated, according to the Van't Hoff equation, to be -24.05 kJ/mol and 30.23 J/mol/K, respectively. The effects of common ions on the binding constant of the HEA-HSA complex at room temperature were also investigated.

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Section: Mechanism Of Binding and Binding Parametersmentioning

confidence: 90%

Investigation of interaction between human serum albumin and N⁶‐(2‐hydroxyethyl)‐adenosine by fluorescence spectroscopy and molecular modelling

et al. 2007

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“…The study of drug-serum albumin binding affinity is helpful to understand the availability of the drug for diffusion or transport to the drug's target organ, as only the free (unbound) drug is capable of diffusion across membranes (17). At present, there have been several studies on the binding process between glycyrrhizin or glycyrrhetic acid with serum albumin (18)(19)(20). However, the structure-affinity relationship in the interactions of triterpenoids with serum albumin and the effect of different substituents at the C-3 position of oleanane-type triterpenoids on binding characteristics with serum albumin have not been clarified.…”

Section: Introductionmentioning

confidence: 99%

Spectroscopic analysis on structure–affinity relationship in the interactions of different oleanane‐type triterpenoids with bovine serum albumin

et al. 2014

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Oleanane-type triterpenoids serve as an important group of plant secondary metabolites with a variety of biological activities and the C-3 position substitution pattern is a significant structural feature for their biological activities. Three selected oleanane-type triterpenoids (glycyrrhizin, glycyrrhetinic acid, and carbenoxolone) bearing different substituents (glucuronic acid dimer, hydroxyl, and succinyl groups) at the C-3 position were studied for their affinities to bind bovine serum albumin (BSA) by steady-state fluorescence, synchronous, three-dimensional fluorescence and ultraviolet-visible (UV-vis) absorption spectra. The binding mechanism of the triterpenoids to BSA is due to the formation of the triterpenoids-BSA complex and the binding affinity is strongest for carbenoxolone and ranked in the order carbenoxolone > glycyrrhetinic acid > glycyrrhizin. The thermodynamic parameters calculated at different temperatures showed that triterpenoids binding to BSA primarily depended on hydrophobic interaction and hydrogen bonding. The distance between the bound triterpenoid and BSA was determined on the basis of the Förster's energy transfer theory. Displacement experiments using phenylbutazone and ibuprofen showed the binding site of triterpenoids on BSA at subdomain IIA (Sudlow's site I). The effect of triterpenoids on BSA conformation was analyzed by UV-vis absorption, and synchronous and three-dimensional fluorescence spectra. These results revealed that the C-3 position substitution pattern significantly affects the structure-affinity relationships of oleanane-type triterpenoid binding to BSA and further affects the bioavailability of triterpenoids in the blood circulatory system.

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“…The UV absorbance showed an increase with the increase in drug concentration, also a shift (blue -shift) in peak could be observed on the interaction of albumin with these drugs and the existence of the equilibrium as: These two changes are indication of a complex formation between albumin and drug (13,14).…”

Section: Results and Discussion Absorption Spectroscopymentioning

confidence: 91%

Thermodynamic Studies for the Interaction of Some Anticoagulant Drugs with Albumin

Al-Rufaie¹,

Al-Shareefi²

2015

JNUS

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Fluorescence spectroscopy in combination with UV-vis absorption spectroscopy was employed to investigate the binding of some important anticoagulant drugs warfarin, heparin and aspirin to human serum albumin under physiological conditions. Scatchard equation provide a measure of the binding affinity between these three drugs individually and albumin. The results of thermodynamic parameters ∆G, ∆H, and ∆S at three different temperatures indicate that the hydrophobic interaction plays a major role for the interaction between each of these drugs and albumin.

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Study of the interaction between monoammonium glycyrrhizinate and bovine serum albumin

Cited by 601 publications

References 20 publications

Investigation of interaction between human serum albumin and N⁶‐(2‐hydroxyethyl)‐adenosine by fluorescence spectroscopy and molecular modelling

Investigation of interaction between human serum albumin and N⁶‐(2‐hydroxyethyl)‐adenosine by fluorescence spectroscopy and molecular modelling

Spectroscopic analysis on structure–affinity relationship in the interactions of different oleanane‐type triterpenoids with bovine serum albumin

Thermodynamic Studies for the Interaction of Some Anticoagulant Drugs with Albumin

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Study of the interaction between monoammonium glycyrrhizinate and bovine serum albumin

Cited by 601 publications

References 20 publications

Investigation of interaction between human serum albumin and N6‐(2‐hydroxyethyl)‐adenosine by fluorescence spectroscopy and molecular modelling

Investigation of interaction between human serum albumin and N6‐(2‐hydroxyethyl)‐adenosine by fluorescence spectroscopy and molecular modelling

Spectroscopic analysis on structure–affinity relationship in the interactions of different oleanane‐type triterpenoids with bovine serum albumin

Thermodynamic Studies for the Interaction of Some Anticoagulant Drugs with Albumin

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Investigation of interaction between human serum albumin and N⁶‐(2‐hydroxyethyl)‐adenosine by fluorescence spectroscopy and molecular modelling

Investigation of interaction between human serum albumin and N⁶‐(2‐hydroxyethyl)‐adenosine by fluorescence spectroscopy and molecular modelling