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Related Experiment Videos

Enantioselective gallopamil protein binding

A S Gross1, C Eser, G Mikus

  • 1Dr. Margarete Fischer-Bosch-Institut für Klinische Pharmakologie, Stuttgart, Germany.

Chirality
|January 1, 1993
PubMed
Summary
This summary is machine-generated.

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Gallopamil enantiomer protein binding is concentration-independent and stereoselective, favoring the (R)-enantiomer. Metabolites do not affect binding, ensuring consistent drug disposition after oral administration.

Area of Science:

  • Pharmacokinetics
  • Drug Metabolism and Disposition
  • Biochemistry

Background:

  • Understanding drug enantiomer protein binding is crucial for predicting pharmacokinetics.
  • Gallopamil, a calcium channel blocker, exists as R- and S-enantiomers with potentially different pharmacological profiles.
  • Human serum albumin (HSA) and alpha 1-acid glycoprotein (AAG) are major plasma proteins involved in drug binding.

Purpose of the Study:

  • To investigate the protein binding characteristics of gallopamil enantiomers in human serum albumin, alpha 1-acid glycoprotein, and serum.
  • To determine if gallopamil enantiomer binding is concentration-dependent or stereoselective.
  • To assess the impact of metabolites and enantiomer-enantiomer interactions on gallopamil protein binding.

Main Methods:

Related Experiment Videos

  • In vitro studies using human serum albumin (HSA), alpha 1-acid glycoprotein (AAG), and human serum.
  • Measurement of fraction bound (fb) for R- and S-gallopamil enantiomers across various concentrations.
  • Ex vivo analysis of protein binding in serum samples collected after oral administration of pseudoracemic gallopamil.

    • Main Results:

    • Gallopamil enantiomer binding to HSA, AAG, and serum proteins was independent of gallopamil concentration within the therapeutic range.
    • Stereoselective binding was observed, with the (R)-enantiomer showing higher binding fractions than the (S)-enantiomer.
    • Protein binding of both enantiomers was not affected by their optical antipodes or by metabolites formed during first-pass metabolism.

    Conclusions:

    • Gallopamil enantiomer protein binding is concentration-independent and stereoselective, favoring the (R)-enantiomer.
    • The observed binding characteristics are consistent both in vitro and ex vivo, suggesting predictable drug disposition.
    • These findings indicate that enantiomer-enantiomer interactions and metabolites do not significantly alter gallopamil's protein binding profile at therapeutic concentrations.