Binding of cadmium(II) and zinc(II) to human and dog serum albumins. An equilibrium dialysis and 113Cd-NMR study

1991 ◽  
Vol 69 (12) ◽  
pp. 809-820 ◽  
Author(s):  
William Goumakos ◽  
Jean-Pierre Laussac ◽  
Bibudhendra Sarkar
Keyword(s):  
Serum Albumin ◽  
Human Serum ◽  
Binding Sites ◽  
Metal Ion ◽  
Equilibrium Dialysis ◽  
Scatchard Analysis ◽  
Serum Albumins ◽  
High Affinity ◽  
Nmr Study ◽  
Nmr Techniques

The binding of Cd(II) and Zn(II) to human serum albumin (HSA) and dog serum albumin (DSA) has been studied by equilibrium dialysis and 113Cd(II)-NMR techniques at physiological pH. Scatchard analysis of the equilibrium dialysis data indicate the presence of at least two classes of binding sites for Cd(II) and Zn(II). On analysis of the high-affinity class of sites, HSA is shown to bind 2.08 ± 0.09 (log K = 5.3 ± 0.6) and 1.07 ± 0.12 (log K = 6.4 ± 0.8) moles of Cd(II) and Zn(II) per mole of protein, respectively. DSA bound 2.02 ± 0.19 (log K = 5.1 ± 0.8), and 1.06 ± 0.15 (log K = 6.0 ± 0.2) moles of Cd(II) and Zn(II) per mole of protein, respectively. Competition studies indicate the presence of one high-affinity Cd(II) site on both HSA and DSA that is not affected by Zn(II) or Cu(II), and one high-affinity Zn(II) site on both HSA and DSA that is not affected by Cd(II) or Cu(II). 113Cadmium-HSA spectra display three resonances corresponding to three different sites of complexation. In site I, Cd(II) is most probably coordinated to two or three histidyl residues, site II to one histidyl residue and three oxygen ligands (carboxylate), while for the most upfield site III, four oxygens are likely to be involved in the binding of the metal ion. The 113Cd(II)-DSA spectra display only two resonances corresponding to two different sites of complexation. The environment around Cd(II) at sites I and II on DSA is similar to sites I and II, respectively, on HSA. No additional resonances are observed in any of these experiments and in particular in the low field region where sulfur coordination occurs. Overall, our results are consistent with the proposal that the physiologically important high-affinity Zn(II) and Cd(II) binding sites of albumins are located not at the Cu(II)-specific NH2-terminal site, but at internal sites, involving mostly nitrogen and oxygen ligands and no sulphur ligand.Key words: albumin, human serum, dog serum, cadmium, zinc, copper, NMR, equilibrium dialysis, binding.

scholarly journals Octanoate binding to the indole- and benzodiazepine-binding region of human serum albumin

1991 ◽  
Vol 273 (3) ◽  
pp. 641-644 ◽  
Author(s):  
U Kragh-Hansen
Keyword(s):  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Equilibrium Dialysis ◽  
Affinity Binding ◽  
Experimental Conditions ◽  
High Affinity Binding ◽  
Molar Ratios ◽  
High Affinity ◽  
High Affinity Binding Site

Binding of L-tryptophan, diazepam and octanoate to defatted human serum albumin was studied at pH 7.0 by equilibrium dialysis at low ligand/protein molar ratios. L-Tryptophan binding takes place at only one site of the protein with an association constant of 4.4 x 10(4) M-1. Under the present experimental conditions, binding of diazepam and octanoate could be accounted for by high-affinity binding alone with primary association constants of 3.8 x 10(5) M-1 and 1.6 x 10(6) M-1 respectively. During the simultaneous presence of L-tryptophan plus octanoate or diazepam plus octanoate, pronounced mutual reductions in binding were observed. Analysis of the data suggests that the reductions in binding represent competition for a common high-affinity binding site. Thus a region seems to exist that is capable of binding one molecule of these diverse ligands with a high affinity. The location of this region within the albumin molecule is discussed.

scholarly journals Studies on the mechanism of binding of serum albumins to immobilized cibacron blue F3G A

1980 ◽  
Vol 189 (1) ◽  
pp. 27-34 ◽  
Author(s):  
R J Leatherbarrow ◽  
P D Dean
Keyword(s):  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Binding Sites ◽  
Serum Albumins ◽  
Fatty Acid Binding ◽  
Cibacron Blue ◽  
Structural Analogues ◽  
Bilirubin Binding ◽  
Sepharose 4B

The interaction of Cibacron Blue F3G A-Sepharose 4B with several serum albumins was studied. Although all albumins used were fond to bind to this adsorbent, human serum albumin was bound to a far greater extent than were the others. From the results of competition experiments and n.m.r. studies of Cibacron Blue and/or bilirubin binding to human serum albumin it is proposed that the mechanism of the interaction between human serum albumin and cibacron Blue is consistent wit Cibacron Blue binding to bilirubin-binding sites. In contrast with these findings with human serum albumin, there is little or no interaction of Cibacron Blue and the bilirubin-binding sites of albumins from rabbit, horse, bovine or sheep sera, although some interaction occurs between Cibacron Blue and the fatty acid-binding sites of these proteins. Structural analogues of Cibacron Blue have been used to investigate the binding of albumins to these ligands.

scholarly journals A Comparative Study on the Interaction of Sulfonamide and Nanosulfonamide with Human Serum Albumin

2013 ◽  
Vol 2013 ◽  
pp. 1-4
Author(s):  
G. Rezaei Behbehani ◽  
Moayed Hossaini Sadr ◽  
H. Nabipur ◽  
L. Barzegar
Keyword(s):  
Human Serum Albumin ◽  
Comparative Study ◽  
Serum Albumin ◽  
Human Serum ◽  
Binding Sites ◽  
Equilibrium Constants ◽  
Antioxidant Property ◽  
Binding Parameters ◽  
High Affinity ◽  
Enthalpy And Entropy

Binding parameters of the N-phenyl benzene sulfonyl hydrazide, sulfonamide, and nanosulfonamide interaction with human serum albumin were determined by calorimetry method. The obtained binding parameters indicated that sulfonamide in the second binding sites has higher affinity for binding than the first binding sites. The binding process of sulfonamide to HSA is both enthalpy and entropy driven. The associated equilibrium constants confirm that sulfonamide binds to HSA with high affinity (2.2×106and 3.86105 M−1for first and second sets of binding sites, resp.). The obtained results indicate that sulfonamide increases the HSA antioxidant property. Nanosulfonamide has much more affinity for HSA (3.6×106 M−1) than sulfonamide.

Quantitative analyses of the interaction between calcium ions and human serum albumin

1993 ◽  
Vol 39 (2) ◽  
pp. 202-208 ◽  
Author(s):  
U Kragh-Hansen ◽  
H Vorum
Keyword(s):  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Calcium Binding ◽  
Equilibrium Dialysis ◽  
Extensive Study ◽  
Scatchard Analysis ◽  
Quantitative Analyses ◽  
Piperazineethanesulfonic Acid ◽  
Ethanesulfonic Acid

Abstract We examined the suitability of nine organic buffers for studying calcium binding to albumin by equilibrium dialysis. Results obtained with defatted human serum albumin showed that 4-(2-hydroxyethyl)-1-piperazineethanesulfonic acid (HEPES) and 2-([tris(hydroxymethyl)methyl] amino)ethanesulfonic acid were superior. Scatchard analysis of the experimental data from an extensive study performed in HEPES at pH 7.4 and 20 degrees C revealed (putting n(i) = 1, i = 1-4) k1 = 367 L/mol, k2 = 314 L/mol, k3 = 291 L/mol, and k4 = 179 L/mol. The very weak binding was characterized as n5 = 10 and k5 = 40 L/mol. The results were also analyzed in terms of stoichiometric association constants. The constants K1 and K2 were calculated to be 1513 and 647 L/mol, respectively, whereas the other constants were considered undeterminable. pH studies showed that in the interval 6.8-7.4, binding was not influenced by changes in acidity. Increasing pH to above the physiological value resulted in increased binding. At pH 8.0, k1 was increased almost fourfold, whereas k2 and k3 were approximately doubled. These findings indicate that the neutral to basic transition is important for the calcium-binding properties of albumin. The transition is a reversible, gradual conformational change of the protein at pH 6-9.

Interaction of 4-Nitroaniline with Serum Albumin

2014 ◽  
Vol 522-524 ◽  
pp. 337-340
Author(s):  
Yan Qiu Liang ◽  
Ying Zhang
Keyword(s):  
Hydrogen Bond ◽  
Human Serum Albumin ◽  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Binding Constants ◽  
Positive Entropy ◽  
Serum Albumins ◽  
High Affinity ◽  
Tryptophan Residues

Bovine serum albumin (BSA) and human serum albumin (HSA) interaction with 4-nitroaniline was investigated by fluorescence spectroscopy respectively. 4-Nitroaniline can strongly quench intrinsic fluorescence of BSA and HSA. 4-Nitroaniline exhibits a high affinity to bovine and human serum albumins. The binding constantsKand the number binding sitenwere obtained by double-log regression equation. Negative enthalpy (ΔH) and positive entropy (ΔS) values indicated that both hydrogen bond and hydrophobic forces played a major role in the binding of 4-nitroaniline and SA. The results of synchronous fluorescence showed the polarity around tryptophan residues was decreased and the hydrophobicity was increased.

scholarly journals Relations between high-affinity binding sites of markers for binding regions on human serum albumin

1985 ◽  
Vol 225 (3) ◽  
pp. 629-638 ◽  
Author(s):  
U Kragh-Hansen
Keyword(s):  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Binding Sites ◽  
Affinity Binding ◽  
Phenol Red ◽  
Coupling Constant ◽  
High Affinity Binding ◽  
High Affinity ◽  
High Affinity Binding Site

Binding of warfarin, digitoxin, diazepam, salicylate and Phenol Red, individually or in different pair combinations, to defatted human serum albumin at ligand/protein molar ratios less than 1:1 was studied at pH 7.0. The binding was determined by ultrafiltration. Some of the experiments were repeated with the use of equilibrium dialysis in order to strengthen the results. Irrespective of the method used, all ligands bind to one high-affinity binding site with an association constant in the range 10(4)-10(6) M-1. High-affinity binding of the following pair of ligands took place independently: warfarin-Phenol Red, warfarin-diazepam, warfarin-digitoxin and digitoxin-diazepam. Simultaneous binding of warfarin and salicylate led to a mutual decrease in binding of one another, as did simultaneous binding of digitoxin and Phenol Red. Both effects could be accounted for by a coupling constant. The coupling constant is the factor by which the primary association constants are affected; in these examples of anti-co-operativity the factor has a value between 0 and 1. In the first example it was calculated to be 0.8 and in the latter 0.5. Finally, digitoxin and salicylate were found to compete for a common high-affinity binding site. The present findings support the proposal of four separate primary binding sites for warfarin, digitoxin (and salicylate), diazepam and Phenol Red. An attempt to correlate this partial binding model for serum albumin with other models in the literature is made.

Serum Albumins Guided Plasmonic Nanoassemblies with Opposite Chiralities

Soft Matter ◽  
2021 ◽  
Author(s):  
Zhaoyi Wang ◽  
Ningning Zhang ◽  
Jincheng Li ◽  
Jun Lu ◽  
Li Zhao ◽  
...  
Keyword(s):  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Great Promise ◽  
Plasmonic Nanostructures ◽  
Serum Albumins ◽  
Catalytic Applications

Chiral assemblies by combining natural biomolecules with plasmonic nanostructures hold great promise for plasmonic enhanced sensing, imaging, and catalytic applications. Herein, we demonstrate that human serum albumin (HSA) and porcine...

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