Enantioselective plasma protein binding of bimoclomol

Júlia Visy, Ilona Fitos, György Mády, László Ürge, Péter Krajcsi, Miklós Simonyi

Research output: Contribution to journalArticle

11 Citations (Scopus)

Abstract

The binding of bimoclomol enantiomers to human plasma, its components, as well as to plasma from monkey, dog, rat, and mouse was investigated by ultrafiltration and equilibrium dialysis. The considerably stronger binding of the (-)-(S)-enantiomer found in human plasma is due to the alpha1-acid glycoprotein (AAG) component. The binding parameters for AAG (nRKR = 1.3 × 104 M-1 and nSKS = 1.0 × 105 M-1) revealed high enantioselectivity, while the binding to human serum albumin was found to be weak (nK = 5 × 103 M-1) and not stereoselective. (-)-(S)-Bimoclomol was extensively displaced in the presence of specific marker ligands for the "FIS" subfraction of human AAG. Comparative binding studies indicated considerable differences between plasma of the five species investigated.

Original languageEnglish
Pages (from-to)638-642
Number of pages5
JournalChirality
Volume14
Issue number8
DOIs
Publication statusPublished - Aug 3 2002

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Keywords

  • Chiral analysis
  • Diabetic complications
  • Glycoprotein subfractions
  • Orosomucoid
  • Stereoselectivity

ASJC Scopus subject areas

  • Analytical Chemistry
  • Catalysis
  • Pharmacology
  • Drug Discovery
  • Spectroscopy
  • Organic Chemistry

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