The fluorescence spectroscopic studies on the interaction of novel aminophosphinic acids with bovine serum albumin

Kaboudin, Babak; Moradi, Khavar; Faghihi, Mohammad Reza; Mohammadi, F.

doi:10.1016/j.jlumin.2013.01.028

Cited by 31 publications

(15 citation statements)

References 39 publications

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“…According to Förster's non‐radiative energy‐transfer theory, the distance( r ) between the donor and the acceptor, critical energy‐transfer distance R 0 when the transfer efficiency is 50% and the energy‐transfer efficiency E can be calculated by the formulas :

E = 1 - F true/ F_{0} = R_{0}^{6} true/ ((), R_{0}^{6} + r^{6})

R_{0}^{6} = 8.79 \times 10^{prefix- 25} K^{2} normalΦ N^{prefix- 4} J

J = true \sum F ((), λ) ε ((), λ) λ^{4} normalΔ λ true/ true \sum F ((), λ) normalΔ λ

where, F 0 is the fluorescence intensity of the donor, F is the fluorescence intensity for the donor in the presence of the same concentration of acceptor; K 2 is the orientation factor, Φ is the fluorescence quantum yield of the donor in the absence of acceptor, N is the refractive index of the medium; F ( λ ) is the fluorescence intensity of the fluorescence donor at wavelength λ and ε ( λ ) is the molar absorption coefficient of the acceptor at this wavelength. Under these experimental conditions, it has been reported previously that K 2 = 2/3, N = 1.336 and Φ = 0.118 .…”

Section: Resultsmentioning

confidence: 99%

Investigation on the effect of fluorescence quenching of bovine serum albumin by cefoxitin sodium using fluorescence spectroscopy and synchronous fluorescence spectroscopy

Liu

Zhang

et al. 2015

Luminescence

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The reaction mechanism of cefoxitin sodium with bovine serum albumin was investigated using fluorescence spectroscopy and synchronous fluorescence spectroscopy at different temperatures. The results showed that the change of binding constant of the synchronous fluorescence method with increasing temperature could be used to estimate the types of quenching mechanisms of drugs with protein and was consistent with one of fluorescence quenching method. In addition, the number of binding sites, type of interaction force, cooperativity between drug and protein and energy-transfer parameters of cefoxitin sodium and bovine serum albumin obtained from two methods using the same equation were consistent. Electrostatic force played a major role in the conjugation reaction between bovine serum albumin and cefoxitin sodium, and the type of quenching was static quenching. The primary binding site for cefoxitin sodium was sub-hydrophobic domain IIA, and the number of binding sites was 1. The value of Hill's coefficients (nH ) was approximately equal to 1, which suggested no cooperativity in the bovine serum albumin-cefoxitin sodium system. The donor-to-acceptor distance r < 7 nm indicated that static fluorescence quenching of bovine serum albumin by cefoxitin sodium was also a non-radiation energy-transfer process. The results indicated that synchronous fluorescence spectrometry could be used to study the reaction mechanism between drug and protein, and was a useful supplement to the conventional method. Copyright © 2015 John Wiley & Sons, Ltd.

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E = 1 - F true/ F_{0} = R_{0}^{6} true/ ((), R_{0}^{6} + r^{6})

R_{0}^{6} = 8.79 \times 10^{prefix- 25} K^{2} normalΦ N^{prefix- 4} J

J = true \sum F ((), λ) ε ((), λ) λ^{4} normalΔ λ true/ true \sum F ((), λ) normalΔ λ

Section: Resultsmentioning

confidence: 99%

Investigation on the effect of fluorescence quenching of bovine serum albumin by cefoxitin sodium using fluorescence spectroscopy and synchronous fluorescence spectroscopy

Liu

Zhang

et al. 2015

Luminescence

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“…To confirm the quenching mechanism induced by cefepime hydrochloride, fluorescence quenching data are analyzed with the Stern-Volmer equation (Equation 1) [26][27][28][29][30][31][32][33][34][35][36][37]:…”

Section: Resultsmentioning

confidence: 99%

Studies on the Interaction of Cefepime Hydrochloride with Bovine Serum Albumin by Fluorescence, Synchronous Fluorescence, Three-Dimensional Fluorescence and Circular Dichroism

Li¹

2017

J Bioanal Biomed

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“…When the temperature change is not very large, the ΔH of a system can be regarded as constant . The thermodynamic parameters can be calculated on the basis of the van't Hoff equation :

R normalln K = normalΔ S - normalΔ H true/ T

normalΔ G = - R T normalln K = normalΔ H - T normalΔ S

…”

Section: Resultsmentioning

confidence: 99%

Using resonance light scattering and UV/vis absorption spectroscopy to study the interaction between gliclazide and bovine serum albumin

Zhang

Liu

et al. 2015

Luminescence

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At different temperatures (298, 310 and 318 K), the interaction between gliclazide and bovine serum albumin (BSA) was investigated using fluorescence quenching spectroscopy, resonance light scattering spectroscopy and UV/vis absorption spectroscopy. The first method studied changes in the fluorescence of BSA on addition of gliclazide, and the latter two methods studied the spectral change in gliclazide while BSA was being added. The results indicated that the quenching mechanism between BSA and gliclazide was static. The binding constant (Ka ), number of binding sites (n), thermodynamic parameters, binding forces and Hill's coefficient were calculated at three temperatures. Values for the binding constant obtained using resonance light scattering and UV/vis absorption spectroscopy were much greater than those obtained from fluorescence quenching spectroscopy, indicating that methods monitoring gliclazide were more accurate and reasonable. In addition, the results suggest that other residues are involved in the reaction and the mode 'point to surface' existed in the interaction between BSA and gliclazide. Copyright © 2015 John Wiley& Sons, Ltd.

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The fluorescence spectroscopic studies on the interaction of novel aminophosphinic acids with bovine serum albumin

Cited by 31 publications

References 39 publications

Investigation on the effect of fluorescence quenching of bovine serum albumin by cefoxitin sodium using fluorescence spectroscopy and synchronous fluorescence spectroscopy

Investigation on the effect of fluorescence quenching of bovine serum albumin by cefoxitin sodium using fluorescence spectroscopy and synchronous fluorescence spectroscopy

Studies on the Interaction of Cefepime Hydrochloride with Bovine Serum Albumin by Fluorescence, Synchronous Fluorescence, Three-Dimensional Fluorescence and Circular Dichroism

Using resonance light scattering and UV/vis absorption spectroscopy to study the interaction between gliclazide and bovine serum albumin

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