warfarin and decanoic-acid

warfarin has been researched along with decanoic-acid* in 2 studies

Other Studies

2 other study(ies) available for warfarin and decanoic-acid

ArticleYear
Hydrophobic borneol-based natural deep eutectic solvents as a green extraction media for air-assisted liquid-liquid micro-extraction of warfarin in biological samples.
    Journal of chromatography. A, 2020, Jun-21, Volume: 1621

    In the present study, a new generation of water-immiscible natural deep eutectic solvents (DESs) was synthesized using borneol as a hydrogen-bonding acceptor and decanoic acid, oleic acid, and thymol as a hydrogen-bonding donor in different molar ratios. These green hydrophobic solvents which are chemically stable in aqueous solutions were used as extraction solvents for isolation and pre-concentration of warfarin in biological samples. In this method, fine droplets of DESs were dispersed into the sample solution by using the air-assisted liquid-liquid micro-extraction method to accelerate the cloudy emulsion system formation and increase the mass transfer of the analyte to the DES-rich phase. The borneol based deep eutectic solvent is a worthy generation of the extraction solvents in the ALLME method due to low-cost and less toxicity. A Plackett-Burman design was utilized for screening the experimental parameters. The effective parameters were then optimized by Box-Behnken design (BBD). Optimized extraction conditions were pH of sample solution of 3.9, number of aspiration/dispersion cycles of 15, the volume of DES of 60 μL, and rate and time of centrifuge of 6000 rpm and 10 min, respectively. Under the optimized conditions, the developed NADES-ALLME method exhibited a wide linear range of 5-500 µg L 

    Topics: Adult; Air; Camphanes; Decanoic Acids; Female; Green Chemistry Technology; Humans; Hydrogen Bonding; Hydrophobic and Hydrophilic Interactions; Limit of Detection; Liquid Phase Microextraction; Oleic Acid; Solvents; Thymol; Warfarin; Water

2020
Fatty acid and drug binding to a low-affinity component of human serum albumin, purified by affinity chromatography.
    International journal of peptide and protein research, 1992, Volume: 40, Issue:5

    Binding equilibria for decanoate to a defatted, commercially available human serum albumin preparation were investigated by dialysis exchange rate determinations. The binding isotherm could not be fitted by the general binding equation. It was necessary to assume that the preparation was a mixture of two albumin components about 40% of the albumin having high affinity and about 60% having low affinity. By affinity chromatography we succeeded in purifying the low-affinity component from the mixture. The high-affinity component, however, could not be isolated. We further analyzed the fatty acid and drug binding abilities of the low-affinity component. The fatty acids decanoate, laurate, myristate and palmitate were bound with higher affinity to the mixture than to the low-affinity component. Diazepam was bound with nearly the same affinity to the low-affinity component as to the albumin mixture, whereas warfarin was not bound at all to the low-affinity component.

    Topics: Chromatography, Affinity; Decanoic Acids; Diazepam; Fatty Acids; Humans; Lauric Acids; Myristic Acid; Myristic Acids; Palmitic Acid; Palmitic Acids; Serum Albumin; Warfarin

1992