Binding of vinca alkaloid analogues to human serum albumin and to α1-acid glycoprotein

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Abstract

The binding of a series of vinca alkaloid analogues having eburnane or indolo[2,3-a]quinolizidine skeletons was studied with human serum albumin (HSA) by affinity chromatography and with α1-acid glycoprotein by means of competition experiments. On HSA the binding occurs at the benzodiazepine-indole binding site via hydrophobic interaction and shows slight stereoselectivity preferring the trans isomers. The binding to α1-AGP proved to be highly stereoselective in favour of the trans isomers having 3(S),16(R)eburnane or 1(R),12b(S)indolo[2,3-a]quinolizidine absolute configurations.

Original languageEnglish
Pages (from-to)377-383
Number of pages7
JournalBiochemical Pharmacology
Volume41
Issue number3
DOIs
Publication statusPublished - Feb 1 1991

ASJC Scopus subject areas

  • Biochemistry
  • Pharmacology

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