Interaction of flavokawain B with lysozyme: A photophysical and molecular simulation study

Feroz, Shevin Rizal; Teoh, Yue Jun; Mohamad, Saharuddin Bin; Hong, Sok Lai; Malek, Sri Nurestri Abd; Tayyab, Saad

doi:10.1016/j.jlumin.2014.11.053

Cited by 24 publications

(11 citation statements)

References 46 publications

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“…For static quenching, the relationship between the fluorescence intensity and the concentration of quencher can usually be described using eqn to obtain the binding constant ( K a ) and the number of binging sites ( n ) :

normallog ((), \frac{F_{0} - F}{F}) = n normallog K_{a} + n normallog ({}, ([], D_{t}) - n \frac{F_{0} - F}{F_{0}} ([], B_{t}))

where [ D t ] and [ B t ] are the total concentrations of CPS and protein, respectively. Assuming that the value of n in curved brackets is equal to 1, and the curve of log( F 0 − F )/ F vs. log{[ D t ] − [ B t ]( F 0 − F )/ F 0 } is drawn and fitted linearly, then the value of n can be obtained from the slope of the plot.…”

Section: Resultsmentioning

confidence: 99%

Investigation on the interaction of cefpirome sulfate with lysozyme by fluorescence quenching spectroscopy and synchronous fluorescence spectroscopy

Han

Liu

et al. 2015

Luminescence

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The reaction mechanism of cefpirome sulfate with lysozyme at different temperatures (298, 310 and 318 K) was investigated using fluorescence quenching and synchronous fluorescence spectroscopy under simulated physiological conditions. The results clearly demonstrated that cefpirome sulfate caused strong quenching of the fluorescence of lysozyme by a static quenching mechanism. The binding constants obtained using the above methods were of the same order of magnitude and very similar. Static electric forces played a key role in the interaction between cefpirome sulfate and lysozyme, and the number of binding sites in the interaction was close to 1. The values of Hill's coefficients were > 1, indicating that drugs or proteins showed a very weakly positive cooperativity in the system. In addition, the conclusions obtained from the two methods using the same equation were consistent. The results indicated that synchronous fluorescence spectrometry could be used to study the binding mechanism between drug and protein, and was a useful supplement to the fluorescence quenching method. In addition, the effect of cefpirome sulfate on the secondary structure of lysozyme was analyzed using circular dichroism spectroscopy.

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normallog ((), \frac{F_{0} - F}{F}) = n normallog K_{a} + n normallog ({}, ([], D_{t}) - n \frac{F_{0} - F}{F_{0}} ([], B_{t}))

Section: Resultsmentioning

confidence: 99%

Investigation on the interaction of cefpirome sulfate with lysozyme by fluorescence quenching spectroscopy and synchronous fluorescence spectroscopy

Han

Liu

et al. 2015

Luminescence

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“…To account for the existence of the inner filter effect, the fluorescence intensity values of the samples need to be corrected for their absorption at excitation and emission wavelengths using the relationship equation

F_{c o r} italic= F_{o b s} italic\times 1 0^{((), A_{ex} italic+ A_{e m}) true/ italic2}

where F cor and F obs are the corrected and observed fluorescence intensities, respectively, and A ex and A em are the absorbance values of the system at the excitation and emission wavelengths, respectively. The fluorescence intensity used in this article was corrected.…”

Section: Methodsmentioning

confidence: 99%

Section: Fluorescence Quenching and Synchronous Fluorescencementioning

confidence: 99%

Spectroscopy and molecular docking study on the interaction of daidzein and genistein with pepsin

Nan

Wang²,

Sun

et al. 2016

Luminescence

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The interaction of pepsin with daidzein (Dai) or genistein (Gen) was investigated using spectroscopic techniques under simulated physiological conditions. Dai and Gen can quench the fluorescence of pepsin and the quenching mechanism was a static process. The binding site number n and apparent binding constant K were measured at different temperatures. The thermodynamic parameters ΔΗ, ΔG and ΔS were calculated. The results indicated that van der Waals forces and hydrogen bond formation played major roles in the interaction of Dai or Gen with pepsin. The binding distance between pepsin and Dai or Gen was calculated according to energy transfer theory. The results of synchronous fluorescence spectra showed that the microenvironment and conformation of pepsin were changed. UV absorption and 3D fluorescence spectra showed that the binding interaction disturbed the microenvironment of amino acid residues and induced conformational changes in pepsin. Molecular docking results showed that Dai and Gen entered into the hydrophobic cavity of pepsin and two hydrogen bonds formed between Dai or Gen and pepsin. The results demonstrated that the interaction behavior between Dai and Gen with pepsin was slightly different, which denoted that the 5-hydroxyl group of Gen, to a certain extent, had an effect on ligand binding to proteins. Copyright © 2016 John Wiley & Sons, Ltd.

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“…S1. It is obvious that adding QDs-612 induces gradual quenching of HSA fluorescence with no obvious shift at the emission peak [32].…”

Section: Quenching Mechanism Of Hsa Fluorescencementioning

confidence: 99%

Insights into the effect of N-acetyl-L-cysteine-capped CdTe quantum dots on the structure and activity of human serum albumin by spectroscopic techniques

Sun

Yang

et al. 2015

Journal of Luminescence

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Interaction of flavokawain B with lysozyme: A photophysical and molecular simulation study

Cited by 24 publications

References 46 publications

Investigation on the interaction of cefpirome sulfate with lysozyme by fluorescence quenching spectroscopy and synchronous fluorescence spectroscopy

Investigation on the interaction of cefpirome sulfate with lysozyme by fluorescence quenching spectroscopy and synchronous fluorescence spectroscopy

Spectroscopy and molecular docking study on the interaction of daidzein and genistein with pepsin

Insights into the effect of N-acetyl-L-cysteine-capped CdTe quantum dots on the structure and activity of human serum albumin by spectroscopic techniques

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