Structural Basis of Non-Steroidal Anti-Inflammatory Drug Diclofenac Binding to Human Serum Albumin

2015 ◽  
Vol 86 (5) ◽  
pp. 1178-1184 ◽  
Author(s):  
Yao Zhang ◽  
Philbert Lee ◽  
Shichu Liang ◽  
Zuping Zhou ◽  
Xiaoyang Wu ◽  
...  
Keyword(s):  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Structural Basis ◽  
Inflammatory Drug ◽  
Anti Inflammatory

Association of Valdecoxib, a Nonsteroidal Anti-Inflammatory Drug, with Human Serum Albumin

2013 ◽  
Vol 89 (6) ◽  
pp. 1399-1405 ◽  
Author(s):  
Maria V. Encinas ◽  
Eduardo Lissi ◽  
Claudio Vergara
Keyword(s):  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Inflammatory Drug ◽  
Anti Inflammatory

Anti-Inflammatory Activity in the Low Molecular Weight Fraction of Commercial Human Serum Albumin (LMWF5A)

2015 ◽  
Vol 37 (1) ◽  
pp. 55-67 ◽  
Author(s):  
Gregory W. Thomas ◽  
Leonard T. Rael ◽  
Charles W. Mains ◽  
Denetta Slone ◽  
Matthew M. Carrick ◽  
...  
Keyword(s):  
Molecular Weight ◽  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Weight Fraction ◽  
Inflammatory Activity ◽  
Low Molecular Weight ◽  
Anti Inflammatory

scholarly journals Structural Basis of Alpha Synuclein Assembly Toxicity Inhibition by Human Serum Albumin

2020 ◽  
Vol 118 (3) ◽  
pp. 61a-62a
Author(s):  
Rashik Ahmed ◽  
Jinfeng Huang ◽  
Adree Khondker ◽  
Maikel C. Rheinstadter ◽  
Madoka Akimoto ◽  
...  
Keyword(s):  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Alpha Synuclein ◽  
Structural Basis

scholarly journals Effect of different parameters on the binding of two anti-inflammatory drugs to human serum albumin

1986 ◽  
Vol 24 (4) ◽  
pp. 1031-1037
Author(s):  
Cristina Zona ◽  
Gianna Roscetti ◽  
Francesca Venturelli ◽  
L. Giorgio Roda
Keyword(s):  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Inflammatory Drugs ◽  
Anti Inflammatory

scholarly journals Interaction studies of chiral non-steroidal anti-inflammatory drugs with HSA protein using capillary electrophoresis frontal analysis and electrokinetic chromatography

2015 ◽  
Author(s):  
◽  
Sinegugu Khulu
Keyword(s):  
Capillary Electrophoresis ◽  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Binding Constants ◽  
Binding Energies ◽  
Frontal Analysis ◽  
Drug Concentrations ◽  
Inflammatory Drugs ◽  
Anti Inflammatory

Human Serum Albumin (HSA) predominantly found in the blood plasma proteins, acts as a carrier for many drugs. In the present work binding interactions of eight arylpropionate non-steroidal anti-inflammatory drugs (NSAIDs) were studied with Human Serum Albumin HSA using Capillary Electrophoresis (CE) under physiological conditions. The concentration of HSA was kept constant (525 μM) whereas the drug concentrations were varied between 50-300 μM in each case. The Frontal analysis (FA) and Capillary Zone Electrophoresis (CZE) modes of CE were applied together with a mathematical modelling of the experimental results with a view to obtaining pharmacokinetic properties of each drug. The binding order of the drugs to HSA were established with the three methods together with the mathematical approach. Our studies revealed the presence of more than one binding sites for some of the available drugs. Additionally, molecular docking studies were conducted to establish the binding conformations of drugs in the binding pocket of the HSA. A very good correlation between the computed binding energies (docking) and the experimental binding constants were observed throughout this study. The logK values for all eight drugs were ranging from 3.37 - 4.56 for FA, 3.16 – 4.39 for CZE, and 3.48 – 5.30 for computational studies.

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.

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