Albumin binding constants

Very recently, we also fitted a model for another physiological partition coefficient, the adsorption to human serum albumin. Since the albumin protein has the potential to bind a large portion of drugs in the blood serum, a drug should not bind strongly to albumin in order to be available for the real target. We used a data set of 92 human albumin binding constants published in a white paper by Kier et al. [140] and achieved the model... 

The frontal analysis technique has been used for the determination of enantioselective binding constants of chiral drugs such as warfarin, verapamil, nilvadipine, and semotidil with proteins such as bovine serum albumin (BSA), human serum albumin (HSA), and plasma lipoproteins (45-51). 

In one of the earlier papers, Sun et al. (48) estimated the binding constants of ibuprofen, flurbiprofen, and ketoprofen to HSA and BSA using the mobility-shift mode of ACE. In this case the drugs were actually used as additives to the background buffer to improve the separation of albumin proteins. This is the opposite approach to what is presented in the next... 

J Sowell, JC Mason, L Strekowski, G Patonay. Binding constant determination of drugs toward subdomain IIIA of human serum albumin by near-infrared dye-displacement capillary electrophoresis. Electrophoresis 22 2512-2517, 2001. 

P Sun, A Hoops, RA Hartwick. Enhanced albumin protein separations and protein-drug binding constant measurements using anti-inflammatory drugs as run buffer additives in affinity capillary elctrophoresis. J Chromatogr B 661 335-340, 1994. 

Binding Constants (K) for Flavonoid-Serum Albumin Complexes (1 1 Stoichiometry), pH 7.4 Phosphate-NaCI Buffer, 25°C... 

Despite its moderate intensity (binding constants K in the range 10 to 10 the interaction between albumin and flavones and flavonols is strong enough to ensure a... 

Dufour, C. and Dangles, O., Flavonoid-serum albumin complexation determination of binding constants and binding sites by fluorescence spectroscopy, Biochim. Biophys. Acta, 1721, 164, 2005. 

Q 4. A drug, X, has a strong affinity for serum albumin. When X was bound to albumin, an increase in absorbance was noted. The v values were determined from these absorbance measurements. Use the data below to determine Kf and n for the interaction between X and albumin. Prepare two types of graphs and compare the results. In one graph plot v versus [X], and in the second plot u/[X] versus v. Which is the better method for calculating binding constants Why ... 

The secondary bonds, which may be formed much more slowly than the primary bonds, actually contribute more to the overall affinity. For example, the primary (Coulombic) bond between bovine serum albumin (BSA) and anti-BSA IgG is 3.3kcalM 1 whereas the secondary bond (van der Waals) is 28kJ, for a total AH = 42 kJ. Because the formation of the secondary bond is much slower, it is easier to prevent formation of the strong complex rather than to try to dissociate it. This is one reason why the competitive immunoassays yield results that correlate with the equilibrium-binding constants, but any such direct-binding assays have to rely on the measurement of the initial rate of binding. 

Protein G contains several binding sites for the constant region of the heavy chain of IgG and also a binding site for serum albumin (15). There are recombinant versions of protein G where the albumin-binding site has been removed and these are preferable for use in purification procedures. 

The following data were obtained for the binding of coumarin to human albumin at 20°C. Determine the binding sites per protein molecule and their binding constants. 

Calculate the binding constants and the number of binding sites of human serum albumin. 

The binding constant between FITC-labeled bovine serum albumin and its monoclonal antibody was determined using ACE with LIF [14], Interaction of the enzyme cyclophilin with the immunosuppressive drug cyclosporine A was quantitatively assessed by CE with UV detection [15]. In the latter case the authors showed in particular how the difference between the sensitivity of the detector and KD of the studied system can severely hamper the correct determination of binding constants. 

In these experiments, the last two volatile compounds behaved as if they were completely non-volatile. Beyeler and Solms (8) calculated the binding constant (K) for several volatile compounds in the presence of soy protein and bovine serum albumin by the following equation ... 

Selected Binding Constants for Endogenous and Exogenous Ligands with Serum Albumin"... 

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