Multiple binding of bepridil in human blood.

  title={Multiple binding of bepridil in human blood.},
  author={Edith Albengres and Sa{\"i}k Urien and J. F. Pognat and Jean Paul Tillement},
  volume={28 3},
Using radiolabelled bepridil, equilibrium dialysis experiments and direct ligand-binding studies were conducted to characterize the binding of bepridil to some human serum proteins, and to blood cells and platelets, respectively. Bepridil was bound to serum albumin with K = 26 +/- 1.6 X 10(3) mol-1 X 1, n = 1.07 +/- 0.04; to alpha 1-acid glycoprotein with K = 442 +/- 68 X 10(3) mol-1 X 1, n = 0.90 +/- 0.04; and with a lesser extent to lipoproteins and gamma-globulins. Bepridil, propranolol… 
Plasma Protein Binding of Bepridil
Bepridil protein binding was not affected by additions of nonesterified fatty acids and free fractions of bepridil were enhanced by addition of verapamil, nifedipine, diltiazem, disopyramide, and warfarin but only at concentrations above those achieved clinically.
Pharmacokinetics and metabolism of bepridil.
  • L. Benet
  • Medicine, Biology
    The American journal of cardiology
  • 1985
The antimalarial drug halofantrine is bound mainly to low and high density lipoproteins in human serum.
The chromatographic resolution of serum preincubated with halofantrine allowed a quantitative analysis of binding to low density lipoproteins, high density lipoins, alpha 1-acid glycoprotein and albumin using the erythrocyte partitioning technique.
Comparative serum protein binding of anthracycline derivatives
Simulations showed that the total serum binding varied over a broad range from 71% (doxorubicin) to 96% (iododoxorubsicin), and was essentially related to the hydrophobicity of the derivatives.
Determination of the free fraction and relative free fraction of drugs strongly bound to plasma proteins.
Comparisons of free fraction values obtained by the method herein described with those obtained by either ultrafiltration or equilibrium dialysis for two compounds that bind predominantly to albumin and another compound that binds to alpha(1)-acid glycoprotein confirm the method produces identical free fractions in comparison with other established techniques.