An approach based on diffusion to study ligand-macromolecule interaction.

Housaindokht, Mohammad Reza; Bahrololoom, Mahmood; Tarighatpoor, Shirin; Mossavi-Movahedi, Ali A.

doi:10.18388/abp.2002_3779

Cited by 5 publications

(3 citation statements)

References 8 publications

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“…There are several methods for ligand binding investigations. [19][20][21][22][23][24][25][26] Equilibrium dialysis is one of the most general methods for this purpose. A disadvantage of this method is being relatively time consuming and demanding for higher concentration of the sample in the experiment.…”

Section: Resultsmentioning

confidence: 99%

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Thermodynamic and Structural Studies on the Human Serum Albumin in the Presence of a Polyoxometalate

2007

Bulletin of the Korean Chemical Society

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The interaction of a polyoxometal (POM), K 6 SiW 11 Co(H 2 O)O 39 .10H 2 O (K 6) as a Keggin, with human serum albumin (HSA) was studied by different methods and techniques. Binding studies show two sets of binding sites for interaction of POM to HSA. Binding analysis and isothermal calorimetery revealed that, the first set of binding site has lower number of bound ligand per mole of protein (ν), lower Hill constant (n), higher binding constant (K), more negative entropy (ΔS) and more electrostatic interaction in comparison to the second set of binding site. In addition, differential scanning calorimetery (DSC) and spectrophotometery data showed that, there are two energetic domains. The first domain is less stable (lower T m and C p) which corresponds to the tail segment of HSA and another with more stability is related to the head segment of HSA. Polyoxometal also decreases the stability of protein as T m , secondary and tertiary structure as well as quenching of the fluorescence decrease. On other hand, perturbations in tertiary structure are more than secondary structure.

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Section: Resultsmentioning

confidence: 99%

“…Therefore, we present some of necessary equations for this purpose. 21 The first Fick's law states that:…”

Section: Resultsmentioning

confidence: 99%

Thermodynamic and Structural Studies on the Human Serum Albumin in the Presence of a Polyoxometalate

2007

Bulletin of the Korean Chemical Society

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“…Ligand binding to macromolecules has previously been studied by methods such as equilibrium dialysis (28), electrochemistry (29), calorimetery (30), spectrophotometry (31), and fluorescence spectroscopy (32). In this work, isothermal titration calorimetry (ITC), ultraviolet (UV), and circular dichroism (CD) were used to characterize the binding of PS to HSA at pH 1.81, 3.56, and 7.40, and the spectral correction technique (33), and the Langmuir and Temkin isothermal models were used to elucidate the mechanism of interaction.…”

Section: Introductionmentioning

confidence: 99%

Potential Protein Toxicity of Synthetic Pigments: Binding of Poncean S to Human Serum Albumin

Gao

Chen

et al. 2008

Biophysical Journal

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Using various methods, e.g., spectrophotometry, circular dichroism, and isothermal titration calorimetry, the interaction of poncean S (PS) with human serum albumin (HSA) was characterized at pH 1.81, 3.56, and 7.40 using the spectral correction technique, and Langmuir and Temkin isothermal models. The consistency among results concerning, e.g., binding number, binding energy, and type of binding, showed that ion pair electrostatic attraction fixed the position of PS in HSA and subsequently induced a combination of multiple noncovalent bonds such as H-bonds, hydrophobic interactions, and van der Waals forces. Ion pair attraction and H-bonds produced a stable PS-HSA complex and led to a marked change in the secondary structure of HSA in acidic media. The PS-HSA binding pattern and the process of change in HSA conformation were also investigated. The potentially toxic effect of PS on the transport function of HSA in a normal physiological environment was analyzed. This work provides a useful experimental strategy for studying the interaction of organic substances with biomacromolecules, helping us to understand the activity or mechanism of toxicity of an organic compound.

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Potential enzyme toxicity of perfluorooctanoic acid

Chen

Song

et al. 2008

Amino Acids

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Using equilibrium dialysis, isothermal titration calorimetry (ITC) and circular dichroism (CD), the interactions of perfluorooctanoic acid (PFOA) and lysozyme were investigated under normal human physiological conditions, i.e., at pH 4.40, 6.00 and 7.40 at 37 degrees C in 0.15 M electrolyte. A simple and rapid spectrophotometric method was developed for determining PFOA concentrations. Interactions between PFOA and lysozyme were found to result from non-specific non-covalent bonds-F/N and F/O affinity, ion-pair attraction, hydrogen bond, hydrophobic interaction and van der Waals force-and were affected by chemical adsorption to monolayers. The results indicated that binding of PFOA altered the secondary structure and activity of lysozyme. This work provides a useful experimental strategy for research into the enzyme toxicity of organic chemicals, e.g., food additives and organic contaminants, and it may help to elucidate the molecular toxicology of human health risks.

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An approach based on diffusion to study ligand-macromolecule interaction.

Cited by 5 publications

References 8 publications

Thermodynamic and Structural Studies on the Human Serum Albumin in the Presence of a Polyoxometalate

Thermodynamic and Structural Studies on the Human Serum Albumin in the Presence of a Polyoxometalate

Potential Protein Toxicity of Synthetic Pigments: Binding of Poncean S to Human Serum Albumin

Potential enzyme toxicity of perfluorooctanoic acid

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