scholarly journals pH-dependency of basic ligand binding to α1-acid glycoprotein (orosomucoid)

1991 ◽  
Vol 280 (1) ◽  
pp. 277-280 ◽  
Author(s):  
S Urien ◽  
F Brée ◽  
B Testa ◽  
J P Tillement
Keyword(s):  
Hydrophobic Interactions ◽  
Association Constants ◽  
Affinity Binding ◽  
Neutral Form ◽  
Difference Spectra ◽  
Acid Glycoprotein ◽  
High Affinity ◽  
Ph Dependency ◽  
Binding Data ◽  
Protonated Forms

The binding interactions of a series of basic ligands with alpha 1-acid glycoprotein (AAG) were examined as a function of pH. The binding to AAG increased with increasing pH, and the binding data were satisfactorily fitted to a model that incorporates the effect of pH and discriminates the association constants of neutral (non-protonated) and protonated forms of ligands. It was shown that ligands in the neutral form have a markedly higher affinity for AAG than the protonated forms, resulting in a concomitant decrease in the pKa of bound ligands. The u.v.-visible difference spectra generated upon binding of a representative ligand to AAG also showed that there was a contribution to the binding arising from the deprotonation of the ligand. It is suggested that all tested ligands bind similarly to AAG and that hydrophobic interactions dominate high-affinity binding to AAG.

scholarly journals pH-dependence of warfarin binding to α1-acid glycoprotein (orosomucoid)

1993 ◽  
Vol 289 (3) ◽  
pp. 767-770 ◽  
Author(s):  
S Urien ◽  
F Brée ◽  
B Testa ◽  
J P Tillement
Keyword(s):  
Hydrogen Bond ◽  
Binding Site ◽  
Ph Dependence ◽  
Protonated Form ◽  
Association Constants ◽  
Histidine Residue ◽  
Difference Spectra ◽  
Acid Glycoprotein ◽  
Binding Data ◽  
Decreasing Ph

The binding of warfarin to alpha 1-acid glycoprotein (AAG) was found to increase with decreasing pH. The u.v.-visible difference spectra generated upon binding to AAG at pH 5.0 or 7.4 showed warfarin to bind as the anion. Warfarin-binding data were satisfactorily fitted to a model that incorporates the effect of pH and discriminates the association constants of the non-protonated and protonated binding site of the protein. It was shown that AAG-binding site in the protonated form had a markedly higher affinity for warfarin than the non-protonated form, with a pK value of 7.7 +/- 0.1, which is likely to be a histidine residue. Among other possible interactions, it is suggested that ligand binding to AAG involves a reinforced hydrogen bond.

scholarly journals Relations between high-affinity binding sites for l-tryptophan, diazepam, salicylate and Phenol Red on human serum albumin

1983 ◽  
Vol 209 (1) ◽  
pp. 135-142 ◽  
Author(s):  
U Kragh-Hansen
Keyword(s):  
Human Serum Albumin ◽  
Serum Albumin ◽  
Binding Sites ◽  
Association Constants ◽  
The Other ◽  
Affinity Binding ◽  
Phenol Red ◽  
High Affinity Binding ◽  
High Affinity ◽  
High Affinity Binding Site

Binding of L-tryptophan, diazepam, salicylate and Phenol Red to defatted human serum albumin was studied by ultrafiltration at pH 7.0. All ligands bind to one high-affinity binding site with association constants of the order of 10(4)-10(5)M-1. The number of secondary binding sites was found to vary from zero to five, with association constants about 10(3)M-1. Competitive binding studies with different pairs of the ligands were performed. Binding of both ligands was determined simultaneously. L-Tryptophan and diazepam were found to compete for a common high-affinity binding site on albumin. The following combinations of ligands do not bind competitively to albumin: L-tryptophan-Phenol Red, L-tryptophan-salicylate and Phenol Red-salicylate. On the other hand, high-affinity bindings of the three ligands do not take place independently but in such a way that binding of one of the ligands results in a decrease in binding of the other ligands. The decreases in binding are reciprocal and can be accounted for by introducing a coupling constant. The magnitude of the constant is dependent on the ligands being bound. In the present study, the mutual decrease in binding was more pronounced with L-tryptophan-salicylate and Phenol Red-salicylate than with L-tryptophan-Phenol Red.

Design and synthesis of lipid-coupled inositol 1,2,3,4,5,6-hexakisphosphate derivatives exhibiting high-affinity binding for the HIV-1 MA domain

2014 ◽  
Vol 12 (27) ◽  
pp. 5006-5022 ◽  
Author(s):  
Hiroshi Tateishi ◽  
Kensaku Anraku ◽  
Ryoko Koga ◽  
Yoshinari Okamoto ◽  
Mikako Fujita ◽  
...  
Keyword(s):  
Hydrophobic Interactions ◽  
Affinity Binding ◽  
High Affinity Binding ◽  
Design And Synthesis ◽  
High Affinity ◽  
Electrostatic And Hydrophobic Interactions ◽  
Hiv 1

Lipid-coupled inositol 1,2,3,4,5,6-hexakisphosphate binds to HIV-1 MA tightly through both electrostatic and hydrophobic interactions.

Binding of the Nucleoside Transport Inhibitor 4-Nitrobenzylthioinosine to Erythrocyte Membranes

1973 ◽  
Vol 51 (5) ◽  
pp. 666-672 ◽  
Author(s):  
M. A. Pickard ◽  
R. R. Brown ◽  
B. Paul ◽  
A. R. P. Paterson
Keyword(s):  
Binding Sites ◽  
Nucleoside Transport ◽  
Erythrocyte Membranes ◽  
Affinity Binding ◽  
Inhibitor Molecule ◽  
High Affinity Binding ◽  
High Affinity ◽  
Transport Inhibitor ◽  
Binding Data ◽  
Nucleoside Transport Inhibitor

4-Nitrobenzylthioinosine (NBMPR), a potent nucleoside transport inhibitor, was prepared in two radioactive forms and the binding of these to erythrocyte ghosts was studied. Similar binding data were obtained with inhibitor containing 14C in the purine 8-position or in the benzyl 7-position, suggesting that the entire inhibitor molecule was bound. A saturable high-affinity mode of NBMPR binding was apparent; NBMPR bound in this way was not removed by washing, but was displaced by a related inhibitor of nucleoside transport, 2-hydroxy-5-nitrobenzylthioguanosine (HNBTGR). It is postulated that the high-affinity binding sites are the nucleoside transport elements of the erythrocyte membrane. From ghosts treated with 14C-NBMPR under conditions which assured binding of the high affinity type, 14C was recovered by extractions in the form of NBMPR. Thus, this mode of NBMPR binding is reversible and covalent linkages do not appear to be involved. A low affinity mode of NBMPR binding was also demonstrated; this appeared to be a partition of NBMPR between the medium and the membrane substance. This component of bound NBMPR was not displaced by HNBTGR and was removed by washing.

Structure of human α1-acid glycoprotein and its high-affinity binding site

2003 ◽  
Vol 300 (1) ◽  
pp. 41-46 ◽  
Author(s):  
Vladimı́r Kopecký ◽  
Rüdiger Ettrich ◽  
Kateřina Hofbauerová ◽  
Vladimı́r Baumruk
Keyword(s):  
Binding Site ◽  
Affinity Binding ◽  
High Affinity Binding ◽  
Acid Glycoprotein ◽  
High Affinity ◽  
High Affinity Binding Site

scholarly journals The structural basis for high affinity binding of α1-acid glycoprotein to the potent anti-tumour compound UCN-01

2021 ◽  
pp. 101392
Author(s):  
Erik J.B. Landin ◽  
Christopher Williams ◽  
Sara A. Ryan ◽  
Alice Bochel ◽  
Nahida Akter ◽  
...  
Keyword(s):  
Structural Basis ◽  
Affinity Binding ◽  
High Affinity Binding ◽  
Acid Glycoprotein ◽  
High Affinity

Melatonin High-Affinity Binding to Alpha-1-Acid Glycoprotein in Human Serum

Pharmacology ◽  
1997 ◽  
Vol 54 (5) ◽  
pp. 271-275 ◽  
Author(s):  
Didier Morin ◽  
Nicolas Simon ◽  
Petra Deprés-Brummer ◽  
Francis Lévi ◽  
Jean-Paul Tillement ◽  
...  
Keyword(s):  
Human Serum ◽  
Affinity Binding ◽  
High Affinity Binding ◽  
Acid Glycoprotein ◽  
High Affinity
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