Location of Binding Sites on Immobilized Human Serum Albumin for Some Nonsteroidal Anti-Inflammatory Drugs

1995 ◽  
Vol 84 (8) ◽  
pp. 949-952 ◽  
Author(s):  
Sibtain Rahim ◽  
Anne-Franç Oise Aubry
Keyword(s):  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Binding Sites ◽  
Inflammatory Drugs ◽  
Anti Inflammatory

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 In Silico Prediction of Interactions between Site II on Human Serum Albumin and Profen Drugs

2013 ◽  
Vol 2013 ◽  
pp. 1-8 ◽  
Author(s):  
Hideto Isogai ◽  
Noriaki Hirayama
Keyword(s):  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Binding Sites ◽  
Binding Mode ◽  
X Ray ◽  
Docking Simulations ◽  
X Ray Crystallography ◽  
Inflammatory Drugs ◽  
Multiple Template

Since binding of a drug molecule to human serum albumin (HSA) significantly affects the pharmacokinetics of the drug, it is highly desirable to predict the binding affinity of the drug. Profen drugs are a widely used class of nonsteroidal anti-inflammatory drugs and it has been reported that several members of the profen class specifically bind to one of the main binding sites named site II. The actual binding mode of only ibuprofen has been directly confirmed by X-ray crystallography. Therefore, it is of interest whether other profen drugs are site II binders. Docking simulations using multiple template structures of HSA from three crystal structures of complexes between drugs and HSA have demonstrated that most of the currently available profen drugs should be site II binders.

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.

Glycation of human serum albumin by acylglucuronides of nonsteroidal anti-inflammatory drugs of the series of phenylpropionates

Life Sciences ◽  
1999 ◽  
Vol 65 (12) ◽  
pp. PL151-PL156 ◽  
Author(s):  
Hélène Georges ◽  
Isabelle Jarecki ◽  
Patrick Netter ◽  
Jacques Magdalou ◽  
Françoise Lapicque
Keyword(s):  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Inflammatory Drugs ◽  
Anti Inflammatory

scholarly journals Interactions Between Sirolimus and Anti-Inflammatory Drugs: Competitive Binding for Human Serum Albumin

2016 ◽  
Vol 6 (2) ◽  
pp. 227-233 ◽  
Author(s):  
Arash Khodaei ◽  
Soheila Bolandnazar ◽  
Hadi Valizadeh ◽  
Leila Hasani ◽  
Parvin Zakeri-Milani
Keyword(s):  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Competitive Binding ◽  
Inflammatory Drugs ◽  
Anti Inflammatory

scholarly journals A Comprehensive Spectroscopic Analysis of the Ibuprofen Binding with Human Serum Albumin, Part I

2020 ◽  
Vol 13 (9) ◽  
pp. 205
Author(s):  
Anna Ploch-Jankowska ◽  
Danuta Pentak
Keyword(s):  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Conformational Changes ◽  
Effect Of Temperature ◽  
Solution Ph ◽  
Ph Values ◽  
Second Derivatives ◽  
Inflammatory Drugs ◽  
Anti Inflammatory

Human serum albumin (HSA) plays a fundamental role in the human body. It takes part in the transport of exogenic and endogenic substances, especially drugs. Ibuprofen (IBU) is one of the most commonly used non-steroidal anti-inflammatory drugs, used for pain relief, fever relief, and for anti-inflammatory purposes. The binding of ligands with HSA is a significant factor which determines the toxicity and the therapeutic dosages of these substances. The aim of this study was to compare the degree of ibuprofen binding with human serum albumin at various temperatures and protein solution pH values. In order to evaluate conformational changes in HSA caused by interaction with ibuprofen, spectrophotometric (first and second derivatives of the UV-VIS spectrum), and spectrofluorometric analyses were performed concerning the mutual interactions of IBU-HSA. The use of fluorescent spectroscopy allowed for recording fluorescent emissive spectra of HSA (5 × 10−6 mol/dm3) without and with the presence of ibuprofen (1 × 10−5–1 × 10−4 mol/dm3) at temperatures of 308, 310, 312, and 314 K at pH values of 6.5, 6.8, 7.4, 7.8, and 8.1. System fluorescence was excited by radiation of wavelengths of λex = 275 nm and λex = 295 nm. Based on this, original and modified Stern-Volmer, Scatchard, Klotz and Hill curves were determined. The data that were obtained showed a significant effect of temperature and pH of the human serum albumin solution on the strength and type of interaction of ibuprofen with HSA.

Sign in / Sign up

Export Citation Format

Share Document