Characterization of the binding of nevadensin to bovine serum albumin by optical spectroscopic technique

Yu, Zhao-Lian; Li, Daojin; Ji, Baoming; Chen, Jianjun

doi:10.1016/j.molstruc.2008.03.013

Cited by 32 publications

(13 citation statements)

References 24 publications

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“…Yet, few results have been involved in drug binding to BLC. Our group has made many efforts in this direction in current years . However, there is no report on the binding of isorhamnetin to BLC, especially about effect of pH on the interaction between isorhamnetin and BLC.…”

Section: Introductionmentioning

confidence: 99%

Investigation on the interaction between isorhamnetin and bovine liver catalase by spectroscopic techniques under different pH conditions

Yang

2016

Luminescence

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The binding of isorhamnetin to bovine liver catalase (BLC) was first investigated at 302, 310 and 318 K at pH 7.4 using spectroscopic methods including fluorescence spectra, circular dichroism (CD) and UV-vis absorption. Spectrophotometric observations are rationalized mainly in terms of a static quenching process. The binding constants and binding sites were evaluated by fluorescence quenching methods. Enzymatic activity of BLC in the absence and presence of isorhamnetin was measured using a UV/vis spectrophotometer. The result revealed that the binding of isorhamnetin to BLC led to a reduction in the activity of BLC. The positive entropy change and enthalpy change indicated that the interaction of isorhamnetin with BLC was mainly driven by hydrophobic forces. The distance r between the donor (BLC) and acceptor (isorhamnetin) was estimated to be 2.99 nm according to fluorescence resonance energy transfer. Fluorescence, synchronous fluorescence, and CD spectra showed no obvious change in the conformation of BLC upon the binding of isorhamnetin. In addition, the influence of pH on the binding of isorhamnetin to BLC was investigated and the binding ability of the drug to BLC deceased under other pH conditions (pH 9.0, 6.5, 5.0, 3.5, or 2.0) as compared with that at pH 7.4. Copyright © 2016 John Wiley & Sons, Ltd.

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Section: Introductionmentioning

confidence: 99%

Investigation on the interaction between isorhamnetin and bovine liver catalase by spectroscopic techniques under different pH conditions

Yang

2016

Luminescence

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“…It is the major transport protein, which can act as a carrier of endogenous and exogenous ligands [5]. The transportation and distribution of the drugs in vivo are related to their interaction with serum albumin.…”

Section: Introductionmentioning

confidence: 99%

The Spectroscopy Study of the Binding of an Active Ingredient of Dioscorea Species with Bovine Serum Albumin with or without Co²⁺ or Zn²⁺

Bian

Peng

Huang

et al. 2014

Evidence-Based Complementary and Alternative Medicine

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Diosgenin (DIO) is the active ingredient of Dioscorea species. The interaction of DIO with bovine serum albumin (BSA) was investigated through spectroscopic methods under simulated physiological conditions. The fluorescence quenching data revealed that the binding of DIO to BSA without or with Co2+ or Zn2+ was a static quenching process. The presence of Co2+ or Zn2+ both increased the static quenching constants K SV and the binding affinity for the BSA-DIO system. In the sight of the competitive experiment and the negative values of ΔH 0 and ΔS 0, DIO bound to site I of BSA mainly through the hydrogen bond and Van der Waals' force. In addition, the conformational changes of BSA were studied by Raman spectra, which revealed that the secondary structure of BSA and microenvironment of the aromatic residues were changed by DIO. The Raman spectra analysis indicated that the changes of conformations, disulfide bridges, and the microenvironment of Tyr, Trp residues of BSA induced by DIO with Co2+ or Zn2+ were different from that without Co2+ or Zn2+.

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“…The binding ability of drugprotein in blood stream may have a significant impact on distribution, free concentration, and metabolism of drug. Serum albumin (SA) is the most abundant protein in the circulatory system and they have ability to transport multitude ligands such as fatty acids, amino acids, steroids, metal ions, and drugs (Yu et al, 2008).…”

Section: Introductionmentioning

confidence: 99%

Study on the interaction of oxymatrine with bovine serum albumin

Zhu

Sun

et al. 2010

Med Chem Res

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The binding reaction of oxymatrine (OMT) with bovine serum albumin (BSA) was studied by the methods of isothermal titration calorimetry, fluorescence, and circular dichroism (CD) spectroscopy. The thermodynamic results indicated that there were two classes of binding sites on the BSA molecule for OMT molecule. When the drug molecule binding to the first class of sites, the standard changes of enthalpy (DH 1°) and entropy (DS 1°) were (-1.07 ± 0.50) kJ/mol and (98.3 ± 0.50) J/ mol/K, respectively. The possible largest number of binding site (N 1 ) was (10.0 ± 0.20). This type of binding was an enthalpy-entropy synergically driven process. On the second class of binding sites, the standard changes of enthalpy (DH 2°) and entropy (DS 2°) were (1.91 ± 0.03) kJ/ mol and (79.8 ± 0.40) J/mol/K, respectively. The possible largest number of binding site (N 2 ) was (25.0 ± 0.30). This type of binding was entropy driven process. The intrinsic fluorescence of BSA was slightly quenched by the formation of BSA-OMT complex. The CD spectra experiment showed that the a-helix contents of BSA decreased. These revealed that the microenvironment and conformation of BSA were changed in the binding reaction.

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Characterization of the binding of nevadensin to bovine serum albumin by optical spectroscopic technique

Cited by 32 publications

References 24 publications

Investigation on the interaction between isorhamnetin and bovine liver catalase by spectroscopic techniques under different pH conditions

Investigation on the interaction between isorhamnetin and bovine liver catalase by spectroscopic techniques under different pH conditions

The Spectroscopy Study of the Binding of an Active Ingredient of Dioscorea Species with Bovine Serum Albumin with or without Co²⁺ or Zn²⁺

Study on the interaction of oxymatrine with bovine serum albumin

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Characterization of the binding of nevadensin to bovine serum albumin by optical spectroscopic technique

Cited by 32 publications

References 24 publications

Investigation on the interaction between isorhamnetin and bovine liver catalase by spectroscopic techniques under different pH conditions

Investigation on the interaction between isorhamnetin and bovine liver catalase by spectroscopic techniques under different pH conditions

The Spectroscopy Study of the Binding of an Active Ingredient of Dioscorea Species with Bovine Serum Albumin with or without Co2+ or Zn2+

Study on the interaction of oxymatrine with bovine serum albumin

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The Spectroscopy Study of the Binding of an Active Ingredient of Dioscorea Species with Bovine Serum Albumin with or without Co²⁺ or Zn²⁺