Evaluation of the interaction between naringenin and human serum albumin: Insights from fluorescence spectroscopy, electrochemical measurement and molecular docking

Tu, Bao; Wang, Yan; Mi, Ran; Ouyang, Yu; Hu, Yanjun

doi:10.1016/j.saa.2015.04.087

Cited by 54 publications

(22 citation statements)

References 35 publications

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“…The corresponding docking scores p K a for site I (Figure a) of MTX binding to HSA is 7.78 and for site II (Figure b) is 6.93. As a higher score reflects a greater binding constant between the compounds and the docking site, these scores predict that MTX is willing to binding to site I of HSA, which is in accordance with the site‐selective experiments. The hydrogen bonds formed between the amino acid residues of HSA and MTX are depicted in Figure (c,d).…”

Section: Resultsmentioning

confidence: 99%

Insights into the interaction of methotrexate and human serum albumin: A spectroscopic and molecular modeling approach

et al. 2017

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In this study, fluorescence spectroscopy and molecular modeling approaches were employed to investigate the binding of methotrexate to human serum albumin (HSA) under physiological conditions. From the mechanism, it was demonstrated that fluorescence quenching of HSA by methotrexate results from the formation of a methotrexate/HSA complex. Binding parameters calculated using the Stern-Volmer method and the Scatchard method showed that methotrexate binds to HSA with binding affinities in the order 10 L·mol . Thermodynamic parameter studies revealed that the binding reaction is spontaneous, and that hydrogen bonds and van der Waals interactions play a major role in the reaction. Site marker competitive displacement experiments and a molecular modeling approach demonstrated that methotrexate binds with appropriate affinity to site I (subdomain IIA) of HSA. Furthermore, we discuss some factors that influence methotrexate binding to HSA.

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Section: Resultsmentioning

confidence: 99%

Insights into the interaction of methotrexate and human serum albumin: A spectroscopic and molecular modeling approach

et al. 2017

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“…Fluorescence quenching studies were carried out by adding appropriate quantities of chemical stock solutions into the HSA solution (2 ml) to obtain concentrations of 10–60 μmol/L in increments of 10 μmol/L. The final methanol volume in the buffer was <1% and this volume did not affect the stability of the HSA molecule. All solutions were stirred for 5 min, and then used at room temperature to generate the fluorescence spectra.…”

Section: Methodsmentioning

confidence: 99%

Study on the interaction of anti‐inflammatory drugs with human serum albumin using molecular docking, quantitative structure–activity relationship, and fluorescence spectroscopy

2019

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The interaction of 14 anti‐inflammatory drugs with human serum albumin (HSA) was investigated using fluorescence quenching, molecular docking studies, and quantitative structure–activity relationship (QSAR) methodology. Binding of anti‐inflammatory drugs to HSA plays a fundamental role in their transport, distribution, delivery, and elimination. Binding constants of these drugs to HSA, obtained using the fluorescence quenching method, were within the range 0.01 × 104 M−1 (acetaminophen) to 1881.05 × 104 M−1 (meloxicam). Binding sites and binding constants of these anti‐inflammatory drugs were estimated using molecular docking. Inspection of the obtained values for docking score, logKb and Kb, showed that the drugs in this data set have a relatively strong binding constant for HSA. QSAR modelling was applied for binding constants obtained from fluorescence quenching and theoretical molecular descriptors. This modelling led to a linear two‐parameter model with a correlation coefficient of 0.95 and adequate robustness. The descriptor results showed the importance of a bonding network and electronegativity as the discriminative structural factors in binding affinity for the HSA molecule.

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“…The results showed that a strong interaction existed between pepsin and Dai or Gen and a complex was formed between them. As reported, the binding constants of some ligands with pepsin (10 7 -10 8 M -1 ) were higher than those of Dai or Gen with pepsin (37,40). Whereas, lower binding constants (10 3 -10 4 M -1 ) were also reported in several other ligand-pepsin complexes (3)(4)(5).…”

Section: Analysis Of the Binding Equilibriummentioning

confidence: 65%

“…The temperatures chosen were 298, 303 and 310 K so that pepsin did not undergo any structural degradation. The thermodynamic parameters can be determined from the van't Hoff equation :

normalln K = prefix- \frac{true}{Δ italicH} + \frac{true}{Δ italicS}

Δ G = Δ H ‐ T Δ S

where K is the binding constant at the temperature T and R is the gas constant. Values of ΔH and ΔS were calculated from the slope and intercept of the van't Hoff plots of ln K against 1/ T .…”

Section: Resultsmentioning

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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Evaluation of the interaction between naringenin and human serum albumin: Insights from fluorescence spectroscopy, electrochemical measurement and molecular docking

Cited by 54 publications

References 35 publications

Insights into the interaction of methotrexate and human serum albumin: A spectroscopic and molecular modeling approach

Insights into the interaction of methotrexate and human serum albumin: A spectroscopic and molecular modeling approach

Study on the interaction of anti‐inflammatory drugs with human serum albumin using molecular docking, quantitative structure–activity relationship, and fluorescence spectroscopy

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

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