scholarly journals Peptide Mapping Identifies Hotspot Site of Modification in Human Serum Albumin by Methylglyoxal Involved in Ligand Binding and Esterase Activity

2004 ◽  
Vol 280 (7) ◽  
pp. 5724-5732 ◽  
Author(s):  
Naila Ahmed ◽  
Darin Dobler ◽  
Mark Dean ◽  
Paul J. Thornalley
Keyword(s):  
Human Serum Albumin ◽  
Ligand Binding ◽  
Serum Albumin ◽  
Human Serum ◽  
Esterase Activity ◽  
Peptide Mapping

scholarly journals Temperature-Dependent Simultaneous Ligand Binding in Human Serum Albumin

2008 ◽  
Vol 112 (16) ◽  
pp. 4884-4891 ◽  
Author(s):  
Sudarson Sekhar Sinha ◽  
Rajib Kumar Mitra ◽  
Samir Kumar Pal
Keyword(s):  
Human Serum Albumin ◽  
Ligand Binding ◽  
Serum Albumin ◽  
Human Serum ◽  
Temperature Dependent

The effect of non-enzymic glycation on ligand binding to human serum albumin

1987 ◽  
Vol 15 (2) ◽  
pp. 267-268 ◽  
Author(s):  
GERALDINE FITZPATRICK ◽  
P. FINBARR DUGGAN
Keyword(s):  
Human Serum Albumin ◽  
Ligand Binding ◽  
Serum Albumin ◽  
Human Serum

Structural Basis of Drug Recognition by Human Serum Albumin

2020 ◽  
Vol 27 (30) ◽  
pp. 4907-4931 ◽  
Author(s):  
Loris Leboffe ◽  
Alessandra di Masi ◽  
Fabio Polticelli ◽  
Viviana Trezza ◽  
Paolo Ascenzi
Keyword(s):  
Human Serum Albumin ◽  
Ligand Binding ◽  
Serum Albumin ◽  
Human Serum ◽  
Binding Capacity ◽  
Pharmacological Therapy ◽  
Drug Binding ◽  
Structural Basis ◽  
Structural Determinants ◽  
Concurrent Administration

Background: Human serum albumin (HSA), the most abundant protein in plasma, is a monomeric multi-domain macromolecule with at least nine binding sites for endogenous and exogenous ligands. HSA displays an extraordinary ligand binding capacity as a depot and carrier for many compounds including most acidic drugs. Consequently, HSA has the potential to influence the pharmacokinetics and pharmacodynamics of drugs. Objective: In this review, the structural determinants of drug binding to the multiple sites of HSA are analyzed and discussed in detail. Moreover, insight into the allosteric and competitive mechanisms underpinning drug recognition, delivery, and efficacy are analyzed and discussed. Conclusion: As several factors can modulate drug binding to HSA (e.g., concurrent administration of drugs competing for the same binding site, ligand binding to allosteric-coupled clefts, genetic inherited diseases, and post-translational modifications), ligand binding to HSA is relevant not only under physiological conditions, but also in the pharmacological therapy management.

Effect of human serum albumin on drug metabolism: Structural evidence of esterase activity of human serum albumin

2007 ◽  
Vol 157 (2) ◽  
pp. 348-355 ◽  
Author(s):  
Feng Yang ◽  
Chuanbing Bian ◽  
Lili Zhu ◽  
Gengxiang Zhao ◽  
Zixiang Huang ◽  
...  
Keyword(s):  
Human Serum Albumin ◽  
Drug Metabolism ◽  
Serum Albumin ◽  
Human Serum ◽  
Esterase Activity

Effect of cationic gemini surfactant and its monomeric counterpart on the conformational stability and esterase activity of human serum albumin

2018 ◽  
Vol 260 ◽  
pp. 65-77 ◽  
Author(s):  
Mehraj ud din Parray ◽  
Muzaffar Ul Hassan Mir ◽  
Neeraj Dohare ◽  
Neha Maurya ◽  
Abbul Bashar Khan ◽  
...  
Keyword(s):  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Esterase Activity ◽  
Gemini Surfactant ◽  
Conformational Stability ◽  
Cationic Gemini Surfactant
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