Spectroscopic studies of 7, 8-dihydroxy-4-methylcoumarin and its interaction with bovine serum albumin

Hussein, Belal H. M.

doi:10.1016/j.jlumin.2010.12.021

Cited by 65 publications

(12 citation statements)

References 60 publications

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“…Therefore, the quenching constant increases for dynamic quenching while it decreases for static quenching with increasing temperature . To demonstrate the quenching mechanism, the fluorescence quenching data were analyzed using the well‐known Stern–Volmer equation :

F_{0} / F = 1 + K_{normalq} τ_{0} [Q] = 1 + K_{normalSV} [Q]

where F 0 and F are the fluorescence intensity in the absence and presence of quencher, respectively; K q stands for the quenching rate constant of the biomacromolecules; τ 0 is the average lifetime of the biomacromolecules without quenchers with a value of 1 × 10 8 ; K SV is the Stern–Volmer quenching constant and [ Q ] is the concentration of quencher.…”

Section: Resultsmentioning

confidence: 92%

Insights into the binding of paclitaxel to human serum albumin: multispectroscopic studies

Yang

Yuan

et al. 2013

Luminescence

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The interaction of paclitaxel with human serum albumin (HSA) was studied using fluorescence, resonance light scattering, ultraviolet-visible, circular dichroism and Fourier transform infrared spectroscopy at pH 7.4. Fluorescence data revealed that the fluorescence quenching of HSA by paclitaxel was a static quenching procedure. Time-resolved fluorescence data also confirmed the quenching mode, which present a constant decay time of about 5 ns. The binding sites were approximately 1 and the binding constant suggested a weak association (324/M at 298 K), which is helpful for the release of the drug to targeted organs. The thermodynamic parameters, ΔG(○), ΔH° and ΔS° were calculated as - 1.06 × 10(4) J/mol, 361 J/mol per K and 9.7 × 10(4) J/mol respectively at 298 K, suggesting that binding was spontaneous and was driven mainly by hydrophobic interactions. The binding distance between HSA and paclitaxel was determined to be 2.23 nm based on the Förster theory. Analysis of circular dichroism, ultraviolet-visible, three-dimensional fluorescence, Fourier transform infrared and resonance light scattering spectra demonstrated that HSA conformation was slightly altered in the presence of paclitaxel and dimension of the individual HSA molecules were larger after interacting with paclitaxel. These results were confirmed by a molecular docking study.

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F_{0} / F = 1 + K_{normalq} τ_{0} [Q] = 1 + K_{normalSV} [Q]

Section: Resultsmentioning

confidence: 92%

Insights into the binding of paclitaxel to human serum albumin: multispectroscopic studies

Yang

Yuan

et al. 2013

Luminescence

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“…Following FRET, the energy transfer efficiency mainly depends on the factors below: (1) sufficient overlap of the donor (BSA) emission spectrum with the acceptor's (metformin) absorption spectrum, (2) the relative orientation of the acceptor and the donor dipoles and (3) the distance of the acceptor with the donor. 41 In this section, we measured the emission spectrum of BSA-metformin as well as the UV-vis spectrum of metformin. From Figure S3, a large overlap was observed between the absorption spectrum of metformin and the BSA-metformin fluorescence spectrum.…”

Section: Energy Transfer From the Protein To The Drugmentioning

confidence: 99%

<p>Novel Albumin Nanoparticle Enhanced the Anti-Insulin-Resistant-Hepatoma Activity of Metformin</p>

Liu

Lin

et al. 2020

IJN

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Introduction: Metformin is an ideal candidate to treat the liver tumor with insulin resistance because of its good performance in the treatment of type 2 diabetes and the advantage in cancer therapy. We aim to develop a delivery system with higher efficiency than free drug. Methods: Metformin-bovine serum albumin (met-BSA) nanoparticles (NPs) were prepared using the anti-solvent precipitation method with a stabilizer of BSA for particle growth. The therapeutic effect of the drug was tested by the insulin-resistant HepG2 cells and C57BL/6J mice at a glucose starvation condition. The interaction mechanism of the drug and the protein during the formation of the NPs was tested using a series of spectroscopy. Results: Metformin and BSA formed nonporous and spherical particles of about 200 nm with proper lognormal distribution and thermostability. The cellular uptake, as well as the anti-liver cancer activities of met-BSA, was enhanced dramatically compared with the free drug. The thermodynamic studies suggested that the weak binding of metformin to BSA was governed by hydrogen bonds and van der Waals forces. Moreover, the results of synchronous, circular dichroism (CD) and three-dimensional fluorescence demonstrated that the BSA skeleton and chromophore microenvironments were changed in the presence of metformin. Conclusion: Therefore, met-BSA has been proved as a simple yet effective therapeutic agent for cancer with insulin resistance, promising for future clinic translations in cancer treatment.

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“…It can be seen that the n value from the slope of the straight line is 1 for the HSA–amifostine complex, which indicates about one amifostine molecule bound one protein molecule at 297 K. The binding constants obtained at 297 K were K A = 4.49 × 10 4 /M. The association constants calculated for the HSA–amifostine system suggest low‐binding affinity, compared to the other strong ligand–protein complexes .…”

Section: Resultsmentioning

confidence: 91%

Binding of amifostine to human serum albumin: A biophysical study

Sun

Zhao

et al. 2014

Luminescence

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The aim of this present work is to investigate the interaction between amifostine and human serum albumin (HSA) in simulated physiological conditions by spectroscopic methods to reveal potential toxic effects of the drug. The results reflected that amifostine caused fluorescence quenching of HSA through a static quenching process, which was further confirmed by the electrochemical experiments. The binding constants at 290, 297 and 304 K were obtained as 2.53 × 10(5) /M, 8.13 × 10(4) /M and 3.59 × 10(4) /M, respectively. There may be one binding site of amifostine on HSA. The thermodynamic parameters indicated that the interaction between amifostine and HSA was driven mainly by hydrogen bonding and electrostatic forces. Synchronous fluorescence spectra, circular dichroism and Fourier transform infrared spectroscopy results showed amifostine binding slightly changed the conformation of HSA with secondary structural content changes. Förster resonance energy transfer study revealed high possibility of energy transfer with amifostine-Trp-214 distance of 3.48 nm. The results of the present study may provide valuable information for studying the distribution, toxicological and pharmacological mechanisms of amifostine in vivo.

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Spectroscopic studies of 7, 8-dihydroxy-4-methylcoumarin and its interaction with bovine serum albumin

Cited by 65 publications

References 60 publications

Insights into the binding of paclitaxel to human serum albumin: multispectroscopic studies

Insights into the binding of paclitaxel to human serum albumin: multispectroscopic studies

<p>Novel Albumin Nanoparticle Enhanced the Anti-Insulin-Resistant-Hepatoma Activity of Metformin</p>

Binding of amifostine to human serum albumin: A biophysical study

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