Evalution of capillary electrophoresis-frontal analysis for the study of low molecular weight drug-human serum albumin interactions

2002 ◽  
Vol 23 (17) ◽  
pp. 2842-2853 ◽  
Author(s):  
Jesper Østergaard ◽  
Christian Schou ◽  
Claus Larsen ◽  
Niels H. H. Heegaard
Keyword(s):  
Molecular Weight ◽  
Capillary Electrophoresis ◽  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Low Molecular Weight ◽  
Frontal Analysis

scholarly journals Simultaneous Determination of Human Serum Albumin and Low-Molecular-Weight Thiols after Derivatization with Monobromobimane

Molecules ◽  
2021 ◽  
Vol 26 (11) ◽  
pp. 3321
Author(s):  
Katarzyna Kurpet ◽  
Rafał Głowacki ◽  
Grażyna Chwatko
Keyword(s):  
Molecular Weight ◽  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Simultaneous Determination ◽  
Reversed Phase ◽  
Fluorescence Labeling ◽  
Detector Response ◽  
Low Molecular Weight

Biothiols are extremely powerful antioxidants that protect cells against the effects of oxidative stress. They are also considered relevant disease biomarkers, specifically risk factors for cardiovascular disease. In this paper, a new procedure for the simultaneous determination of human serum albumin and low-molecular-weight thiols in plasma is described. The method is based on the pre-column derivatization of analytes with a thiol-specific fluorescence labeling reagent, monobromobimane, followed by separation and quantification through reversed-phase high-performance liquid chromatography with fluorescence detection (excitation, 378 nm; emission, 492 nm). Prior to the derivatization step, the oxidized thiols are converted to their reduced forms by reductive cleavage with sodium borohydride. Linearity in the detector response for total thiols was observed in the following ranges: 1.76–30.0 mg mL−1 for human serum albumin, 0.29–5.0 nmol mL−1 for α-lipoic acid, 1.16–35 nmol mL−1 for glutathione, 9.83–450.0 nmol mL−1 for cysteine, 0.55–40.0 nmol mL−1 for homocysteine, 0.34–50.0 nmol mL−1 for N-acetyl-L-cysteine, and 1.45–45.0 nmol mL−1 for cysteinylglycine. Recovery values of 85.16–119.48% were recorded for all the analytes. The developed method is sensitive, repeatable, and linear within the expected ranges of total thiols. The devised procedure can be applied to plasma samples to monitor biochemical processes in various pathophysiological states.

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

High-throughput capillary electrophoresis frontal analysis method for the study of drug interactions with human serum albumin at near-physiological conditions

2004 ◽  
Vol 25 (1819) ◽  
pp. 3176-3185 ◽  
Author(s):  
Juan J. Martínez-Pla ◽  
María A. Martínez-Gómez ◽  
Yolanda Martín-Biosca ◽  
Salvador Sagrado ◽  
Rosa M. Villanueva-Camañas ◽  
...  
Keyword(s):  
Capillary Electrophoresis ◽  
Human Serum Albumin ◽  
Serum Albumin ◽  
Drug Interactions ◽  
Human Serum ◽  
High Throughput ◽  
Frontal Analysis ◽  
Analysis Method ◽  
Physiological Conditions

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.

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