Equilibrium and kinetic studies of the binding of tri- and tetra-anionic ligands to bovine serum albumin

Murakami, Kiyofumi

doi:10.1016/0301-4622(91)85040-w

Cited by 14 publications

(8 citation statements)

References 31 publications

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“…Methods. The extent of ligand binding was measured using the equilibrium dialysis technique . Visking dialysis tubing (24/32) cut to a length of 9 cm was treated twice with a 1% NaHCO 3 aqueous solution at 100 °C for 40 min, rinsed with distilled water, and subsequently immersed in a 95% aqueous ethanol solution overnight, soaked in a warm 1% ethylenediaminetetraacetic acid (EDTA) solution for 30 min, and finally exhaustively rinsed with distilled water.…”

Section: Methodsmentioning

confidence: 99%

Cooperative Ligand Binding to Globular Protein: A Statistical Mechanical Theory Based on a Simple Geometrical Model and Its Application to Lysozyme Systems

Murakami

1999

Langmuir

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A simple geometrical model for statistical mechanical analysis of cooperative binding of monoionic ligands to globular proteins was developed. It is assumed that the ligand has the charged group, which is able to bind the oppositely charged residues on protein surface by electrostatic interactions, and the hydrophobic region, which causes cooperativity by the interactions between bound ligands. The bound ligand together with the side chain of the ionic residue is assumed to be mobile over the protein surface within the tangential half sphere with the center at the β-carbon of the side chain and the radius of the effective ligand length. The potential around a bound ligand was approximated by the cylindrical square-well potential with an exclusion core along the center line. The shape of protein was assumed to be spherical. The distance between charged residues on the protein surface was taken from crystallographic data. Grand partition function was calculated as the sum of the terms of all possible bound states. In each term, the electrostatic free energy was taken into account as the Debye−Huckel type electrostatic potential energy for the distribution of isolated charges, and the partition function due to hydrophobic and/or stacking interactions was calculated as the product of pairwise interactions. The model was applied to the binding of an anionic azo dye or anionic surfactants to hen egg white lysozyme at several experimental conditions. The calculated binding isotherms well-reproduced the experimental data. The values of the model parameters estimated were consistent with the ligand size and the magnitude of hydrophobic interaction. Other detailed information such as species fraction, variance, and bound fraction of each site was obtained. The results show the wide applicability of the present model theory.

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Section: Methodsmentioning

confidence: 99%

Cooperative Ligand Binding to Globular Protein: A Statistical Mechanical Theory Based on a Simple Geometrical Model and Its Application to Lysozyme Systems

Murakami

1999

Langmuir

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“…The concentration of DNA was determined using a molar absorption coefficient ( ε ) value of 13 200 M −1 cm −1 at 260 nm in base pairs (Graves et al ., ). The concentration of AR 27 was determined using an ε value of 25 600 M −1 cm −1 at 521 nm (Murakami, ). All experiments were performed in 10 mM citrate–phosphate buffer containing 5 mM of Na 2 HPO 4 , pH 7.0.…”

Section: Methodsmentioning

confidence: 99%

Spectroscopic and microcalorimetric studies on the molecular binding of food colorant acid red 27 with deoxyribonucleic acid

Basu

Kumar

2016

J of Molecular Recognition

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Interaction of the food colorant acid red 27 with double stranded DNA was investigated using spectroscopic and calorimetric methods. Absorbance and fluorescence studies suggested an intimate binding interaction between the dye and DNA. The quantum efficiency value testified an effective energy transfer from the DNA base pairs to the dye molecules. Minor groove displacement assay with Hoechst 33258 revealed that the binding occurs in the minor groove of DNA. Circular dichroism studies revealed that acid red 27 induces moderate conformational perturbations in DNA. Results of calorimetric studies suggested that the complexation process was driven largely by positive entropic contribution with a smaller favorable enthalpy contribution. The equilibrium constant of the binding was calculated to be (3.04 ± 0.09) × 10(4) M(-1) at 298.15 K. Negative heat capacity value along with the enthalpy-entropy compensation phenomenon established the involvement of dominant hydrophobic forces in the binding process. Differential scanning calorimetry studies presented evidence for an increased thermal stability of DNA on binding of acid red 27. Copyright © 2016 John Wiley & Sons, Ltd.

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“…The concentrations of HSA and BSA samples were spectrophotometrically determined using molar absorption coefficient values (ε) of 3.66 × 10 4 and 4.38 × 10 4 M –1 cm –1 , respectively, at 280 nm . The concentration of the dye was also determined spectrophotometrically using the ε value of 2.56 × 10 4 M –1 cm –1 reported in the literature . All of the buffer salts were of analytical grade.…”

Section: Methodsmentioning

confidence: 99%

“…28 The concentration of the dye was also determined spectrophotometrically using the ε value of 2.56 × 10 4 M −1 cm −1 reported in the literature. 25 All of the buffer salts were of analytical grade. The aforementioned citrate−phosphate buffer was prepared in triple-distilled and deionized water.…”

Section: ■ Materials and Methodsmentioning

confidence: 99%

“…Binding to serum proteins may be used as a vehicle to regulate and control the available free concentration of the azo dye for toxic action. , Human serum albumin (HSA) and bovine serum albumin (BSA) are two homologous globular heart-shaped proteins having three structurally similar domains (I, II, and III), and each comprises of two subdomains (A and B). − The two most important binding regions in these serum proteins are Sudlow’s site I (subdomain IIA) and site II (subdomain IIIA). , Zhang et al reported that amaranth binds in Sudlow’s site I (subdomain IIA) of HSA . Spectroscopic, ultrafiltration, electrochemical, and kinetic studies on the interaction of amaranth and serum proteins have been already undertaken. ,− Although the structural aspects of the interaction have been studied, the calorimetric studies to elucidate the thermodynamics of the interaction have not yet been performed. Thus, the present work elucidates the thermodynamics of the interaction of amaranth with two homologous serum proteins using isothermal titration calorimetry (ITC) and differential scanning calorimetry (DSC) techniques.…”

Section: Introductionmentioning

confidence: 99%

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Targeting Proteins with Toxic Azo Dyes: A Microcalorimetric Characterization of the Interaction of the Food Colorant Amaranth with Serum Proteins

Basu

Kumar

2014

J. Agric. Food Chem.

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The interaction of amaranth with two homologous serum albumins from human and bovine (HSA and BSA) was studied by microcalorimetry. The binding stoichiometry for the complexation of amaranth to both BSA and HSA was around 1, and the equilibrium constants were (5.79 ± 0.07) × 10(5) and (1.76 ± 0.05) × 10(5) M(-1), respectively. The binding reaction to HSA at 298.15 K was driven by a large negative enthalpic contribution and a small but positive entropic contribution, while to BSA, it was entirely enthalpy-driven and the entropic contribution was unfavorable. Parsing of the standard molar Gibbs energy revealed that the complexation was dominated by non-polyelectrolytic forces. Temperature-dependent isothermal titration calorimetry studies revealed that the enthalpic contribution increased and the entropic contribution decreased with the rise in the temperature but the Gibbs energy change remained almost unaltered. Differential scanning calorimetry results revealed that the binding reaction stabilized the serum albumins significantly against thermal unfolding.

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Equilibrium and kinetic studies of the binding of tri- and tetra-anionic ligands to bovine serum albumin

Cited by 14 publications

References 31 publications

Cooperative Ligand Binding to Globular Protein: A Statistical Mechanical Theory Based on a Simple Geometrical Model and Its Application to Lysozyme Systems

Cooperative Ligand Binding to Globular Protein: A Statistical Mechanical Theory Based on a Simple Geometrical Model and Its Application to Lysozyme Systems

Spectroscopic and microcalorimetric studies on the molecular binding of food colorant acid red 27 with deoxyribonucleic acid

Targeting Proteins with Toxic Azo Dyes: A Microcalorimetric Characterization of the Interaction of the Food Colorant Amaranth with Serum Proteins

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