Development of DNA Nanostructures for High-Affinity Binding to Human Serum Albumin

2017 ◽  
Vol 139 (21) ◽  
pp. 7355-7362 ◽  
Author(s):  
Aurélie Lacroix ◽  
Thomas G. W. Edwardson ◽  
Mark A. Hancock ◽  
Michael D. Dore ◽  
Hanadi F. Sleiman
Keyword(s):  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Affinity Binding ◽  
Dna Nanostructures ◽  
High Affinity Binding ◽  
High Affinity

scholarly journals Biological characteristics of two lysines on human serum albumin in the high-affinity binding of 4Z,15Z-bilirubin-IXα revealed by phage display

FEBS Journal ◽  
2011 ◽  
Vol 278 (21) ◽  
pp. 4100-4111 ◽  
Author(s):  
Ai Minomo ◽  
Yu Ishima ◽  
Ulrich Kragh-Hansen ◽  
Victor T. G. Chuang ◽  
Makiyo Uchida ◽  
...  
Keyword(s):  
Human Serum Albumin ◽  
Serum Albumin ◽  
Phage Display ◽  
Human Serum ◽  
Biological Characteristics ◽  
Affinity Binding ◽  
High Affinity Binding ◽  
High Affinity

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.

Conformational stability and warfarin-binding properties of human serum albumin studied by recombinant mutants

2001 ◽  
Vol 357 (1) ◽  
pp. 269-274 ◽  
Author(s):  
Hiroshi WATANABE ◽  
Ulrich KRAGH-HANSEN ◽  
Sumio TANASE ◽  
Keisuke NAKAJOU ◽  
Maki MITARAI ◽  
...  
Keyword(s):  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Expression System ◽  
Conformational Stability ◽  
Affinity Binding ◽  
Binding Properties ◽  
High Affinity Binding ◽  
Yeast Expression System ◽  
High Affinity

Correctly folded recombinant wild-type human serum albumin and the single-residue mutants K199A, W214A, R218H and H242Q were produced with the use of a yeast expression system. The changes in R218H resulted in a pronounced decrease in intrinsic fluorescence. Thermodynamic parameters for thermal denaturation of the present mutants and of five additional mutants have been determined, showing small increases in stability for two mutants (R218H and H242Q) and a larger decrease in stability for one (W214A). In the last of these, denaturation was a heterogeneous process starting at physiological temperature. The high-affinity binding constant for warfarin at pH7.4 was determined by fluorescence spectroscopy: there was a significant increase in affinity for binding of warfarin to H242Q and K199A and a smaller decrease in affinity for W214A and R218H. The findings show that Trp-214 is not as essential for the high-affinity binding of warfarin as has previously been thought.

scholarly journals High affinity binding of paclitaxel to human serum albumin

2001 ◽  
Vol 268 (7) ◽  
pp. 2187-2191 ◽  
Author(s):  
Krisztina Paál ◽  
József Müller ◽  
Lajos Hegedûs
Keyword(s):  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Affinity Binding ◽  
High Affinity Binding ◽  
High Affinity

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.

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