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At least 1,513 records · Page 84Linked to original sources
PubMed1997

Stereoselectivity and enantiomer-enantiomer interactions in the binding of ibuprofen to human serum albumin.

Binding of ibuprofen (IB) enantiomers to human serum albumin (HSA) was studied using a chiral fluorescent derivatizing reagent, which enabled the measurement of IB enantiomers at a concentration as low 5 x 10(-8) M. Scatchard analyses revealed that there were two classes of binding sites for both enantiomers. For the high affinity site, the number of the binding sites was one for both enantiomers, and the binding constant of R-IB was 2.3-fold greater than that of S-IB. The difference in the affinity at the high affinity site may result in the stereoselective binding of IB enantiomers at therapeutic concentrations. It was confirmed that the high affinity site of IB enantiomers is Site II (diazepam binding site) by using site marker ligands. Also, significant enantiomer-enantiomer interactions were observed in the binding. The binding data were quantitatively analyzed and a binding model with an assumption of competitive interactions only at the high affinity site simulated the binding characteristics of IB enantiomers fairly well.

Anti-Inflammatory Agents, Non-Steroidal↗
PubMed1996

Atrial flutter with 1:1 conduction after administration of the antimalarial drug mefloquine.

Antimalarial drugs are well known for their cardiovascular toxicity. Quinine, the most famous antimalarial agent, mostly causes bradycardia. Quinidine, its dextrorotatory isomer, may cause 1:1 atrioventricular (AV) conduction during atrial flutter. The newly developed drug mefloquine was reported to have fewer cardiac side effects. We describe a 63-year-old male patient with atrial flutter in whom mefloquine use was associated with 1:1 AV conduction, and who then responded to therapy with digoxin and sotalol. The patient had a history of palpitations. This case report emphasizes that mefloquine should be used with caution in patients with a history of palpitations or underlying heart disease.

Antimalarials↗
PubMedDate not supplied

Cardiovascular drug interactions.

Drug interactions may be responsible for certain changes in therapeutic response and toxicity of cardiac drugs. Interactions occur at the sites of drug absorption and elimination as well as at the receptor sites in the pacemaker cells, specialized conducting tissue, and myocardium. Studies of the kinetics of cardiac drugs are being applied clinically in an effort to reduce the danger of adverse drug interactions in heart patients.

Anti-Arrhythmia Agents↗
PubMed1975

Variant HeLa cells selected for their resistance to ouabain.

The cardiac glyoside, ouabain, normally kills HeLa cells at concentrations of about 10-7 M or greater. By treating a population of HeLa cells with increasingly higher concentrations of the drug, a vaiant population was obtained of HeLa cells capable of growing in medium containing 10-4 M ouabain. Inhibition of volume regulation of cells subjected to hypotonic shock was used as a measure of inhibition of active transport of Na across the plasma membrane. In that way of dose-response curves for the rapid effects of ouabain and other inhibitors of active Na transport were obtained with both the original, ouabain-sensitive (OS) and the variant, ouabain-resistant (OR) cells. Three other cardiac glycosides (digoxin, digtoxin and hellebrin) and two aglycones (digitoxigenin and strophanthidin) were found to be equally as effective as ouabain in inhibiting volume regulation of the OS cells; the concentration whichproduced half-maximum inhibition, I(max/2), was about 6X 10-7 M in each case. Similar inhibition of the OR population by ouabain was observed only when the concentration exceeded 10-4 M [I(max/2-2.5 X 10-4 M], and the other steroid compounds had no effect on the variant cells at the highest concentrations tested (-2 X 10-5 M). OR and OS cells different also in their sensitivities to its cardoactive erythrophleum alkaloid, coumingine; I(max/2) for OS and OR cells was 5 X 10-8 M and 6 X 10-7 M, respectively. These results in addition to results of ouabain binding experiments and measurements of the rates of reversal of inhibition of volume regulation, suggest that a major reason for the differential sensitivities of the two phenotypes to these drugs is different affinities of their sodium pumps for inhibitors of active transport.

Alkaloids↗