Capillary electrophoresis frontal analysis for the study of flavonoid interactions with human serum albumin

Knjazeva, Tatjana; Kaljurand, Mihkel

doi:10.1007/s00216-010-3726-4

Cited by 22 publications

(7 citation statements)

References 31 publications

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“…A variety of techniques were reported for the study of protein and phenolic compound interaction, such as equilibrium dialysis, 1,2 ultrafiltration, 3,4 fluorescence spectroscopy, 5 capillary electrophoresis, 6 and isothermal titration calorimetry (ITC). 4,7 Although most techniques are used to probe the kinetic and equilibrium parameters, the ITC method is used to determine the thermodynamic properties as well as equilibrium parameters of protein-ligand interactions.…”

Section: Introductionmentioning

confidence: 99%

Molecular and thermodynamic basis for EGCG‐Keratin interaction‐part II: Experimental investigation

et al. 2013

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In Part I, we reported all-atom, fully solvated molecular dynamics (MD) simulations of epigallocatechin-3-gallate (EGCG) binding to keratin. Herein, we report the second part of experimental investigation on EGCG binding to keratin using ultrafiltration and isothermal titration calorimetry (ITC). The thermodynamic equilibrium of EGCG binding to keratin has been quantitatively determined using ultrafiltration and high-performance liquid chromatography-UV/vis. The relationship confirms multilayer binding of EGCG to keratin which was observed in MD simulations. By combining the ultrafiltration and ITC data, the thermodynamic parameters of EGCG binding to keratin have been quantified. The obtained free energy of the first layer binding (ΔG=-6.37 kcal mol) is shown in excellent agreement with that obtained from computer simulations (ΔG=-6.20 kcal mol) presented in Part I. © 2013 American Institute of Chemical Engineers

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Section: Introductionmentioning

confidence: 99%

Molecular and thermodynamic basis for EGCG‐Keratin interaction‐part II: Experimental investigation

et al. 2013

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“…The displacement studies were performed by using several methods, including ultrafiltration [10], ED [11], crystallographic studies [12], CD [13], fluorescence spectroscopy [14, 15], molecular modeling [16], high‐performance affinity chromatography [17], and capillary electrophoresis (CE) in different modes including affinity CE, vacancy affinity CE, partial filling CE, near‐infrared dye‐displacement CE or CE‐FA [1, 18–21]. Despite the fact that CE‐FA method is widely used for binding parameters determination only a few research groups reported about its applicability for displacement studies [22–29]. CE‐FA method was chosen for these measurements in view of its many benefits, which include small sample consumption, robustness and the possibility of high‐throughput screening [30,31].…”

Section: Introductionmentioning

confidence: 99%

Applicability of capillary electrophoresis‐frontal analysis for displacement studies: Effect of several drugs on l‐tryptophan and lidocaine binding to human serum albumin

Nevídalová

Michalcová

Glatz

2020

J of Separation Science

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The effective concentration of a drug in the blood, i.e. the concentration of a free drug in the blood, is influenced by the strength of drug binding onto plasma proteins. Besides its efficacy, these interactions subsequently influence the liberation, absorption, distribution, metabolism, excretion, and toxicological properties of the drug. It is important to not only determine the binding strength and stoichiometry, but also the binding site of a drug on the plasma protein molecule, because the co-administration of drugs with the same binding site can affect the above-mentioned concentration and as a result the pharmacological behavior of the drugs and lead to side effects caused by the change in free drug concentration, its toxicity. In this study, the binding characteristics of six drugs with human serum albumin, the most abundant protein in human plasma, were determined by capillary electrophoresis-frontal analysis, and the obtained values of binding parameters were compared with the literature data. The effect of several drugs and site markers on the binding of l-tryptophan and lidocaine to human serum albumin was investigated in subsequent displacement studies which thus demonstrated the usability of capillary electrophoresis as an automated high-throughput screening method for drug-protein binding studies.

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“…Noncovalent interaction includes electrostatic interaction, van der Waals interaction, hydrogen bonds, hydrophobic interaction, and π bonds. Noncovalent interaction between protein and phenolic compounds can be studied by various techniques such as equilibrium dialysis (ED), , ultrafiltration, , ultraviolet–visible absorption spectroscopy (UV–vis), , fluorescence spectroscopy, , capillary electrophoresis, and isothermal titration microcalorimetry (ITC). ,, Using ED and ultrafiltration, the thermodynamic equilibrium of phenolic compounds binding to protein can be determined. However, phenolic compounds can also bind to the membrane used.…”

Section: Introductionmentioning

confidence: 99%

Experimental and Theoretical Studies on the Binding of Epigallocatechin Gallate to Purified Porcine Gastric Mucin

et al. 2012

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Binding of epigallocatechin gallate (EGCG) to highly purified short side-chain porcine gastric mucin similar to human MUC6 type has been studied by ultraviolet-visible absorption spectroscopy (UV-vis), ultrafiltration isothermal titration microcalorimetry (ITC) and transmission electron microscopy (TEM). The thermodynamic equilibrium of EGCG binding to mucin has been quantitatively determined using ultrafiltration and high-performance liquid chromatography (HPLC)-UV/vis. The relationship suggests multilayer binding rather than simple Langmuir monolayer binding of EGCG. By combining the ultrafiltration and ITC data, the thermodynamic parameters of EGCG binding to mucin have been obtained. The binding constant for the first layer is about an order of magnitude higher than that of the consecutive multilayers. Negative entropy indicates multilayer of EGCG formed. Hydrogen bonding may be responsible for the multilayer formation. Increasing temperature resulted in a decrease in the binding affinity, further suggesting that hydrogen bonds dominated the interaction energy. A TEM micrograph of the EGCG-mucin complex revealed a monodispersion of blobs similar to pure mucin solution but with relatively bigger size (about twice). It is proposed that the EGCG-mucin binding process occurs by single and/or cluster of EGCG molecules driven to the surface of the two hydrophobic globules of mucin by hydrophobic interaction followed by hydrogen bond interaction between EGCG and mucin. Further adsorption of EGCG molecules onto bound EGCG molecules to form multilayers can also occur. This fits well with the observations that EGCG-mucin interaction followed a multilayer adsorption isotherm, the energy released is dominated by hydrogen bonds, and no large aggregates were formed.

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Capillary electrophoresis frontal analysis for the study of flavonoid interactions with human serum albumin

Cited by 22 publications

References 31 publications

Molecular and thermodynamic basis for EGCG‐Keratin interaction‐part II: Experimental investigation

Molecular and thermodynamic basis for EGCG‐Keratin interaction‐part II: Experimental investigation

Applicability of capillary electrophoresis‐frontal analysis for displacement studies: Effect of several drugs on l‐tryptophan and lidocaine binding to human serum albumin

Experimental and Theoretical Studies on the Binding of Epigallocatechin Gallate to Purified Porcine Gastric Mucin

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