Characterisation of the binding of digitoxin and acetyldigitoxin to human serum albumin by high-performance affinity chromatography

David S. Hage, Arundhati Sengupta

Research output: Contribution to journalArticle

42 Citations (Scopus)

Abstract

Zonal elution and high-performance affinity chromatography were used to examine interactions of the drugs digitoxin and acetyldigitoxin with the protein human serum albumin (HSA). This was done by injecting small amounts of digitoxin and acetyldigitoxin onto an immobilized HSA column in the presence of mobile phases that contained various concentrations of digitoxin, acetyldigitoxin or other solutes as competing agents. A fixed concentration of β-cyclodextrin was also present in the mobile phase as a solubilising agent. It was found that digitoxin and acetyldigitoxin each had strong interactions at a single common binding site on HSA, but with slightly different equilibrium constants for this region. Neither compound showed any competition with warfarin or L-tryptophan, which were used as probes for binding at the warfarin-azapropazone and indole-benzodiazepine sites of HSA. These results confirmed the presence of a separate binding region on HSA for digitoxin-related compounds. Copyright (C) 1999 Elsevier Science B.V.

Original languageEnglish (US)
Pages (from-to)91-100
Number of pages10
JournalJournal of Chromatography B: Biomedical Sciences and Applications
Volume724
Issue number1
DOIs
StatePublished - Mar 5 1999

Fingerprint

Acetyldigitoxins
Digitoxin
Affinity chromatography
Serum Albumin
Warfarin
Apazone
Equilibrium constants
Cyclodextrins
Benzodiazepines
Tryptophan
Binding Sites
Pharmaceutical Preparations

Keywords

  • Acetyldigitoxin
  • Digitoxin
  • Human serum albumin

ASJC Scopus subject areas

  • Chemistry(all)

Cite this

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AU - Sengupta, Arundhati

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N2 - Zonal elution and high-performance affinity chromatography were used to examine interactions of the drugs digitoxin and acetyldigitoxin with the protein human serum albumin (HSA). This was done by injecting small amounts of digitoxin and acetyldigitoxin onto an immobilized HSA column in the presence of mobile phases that contained various concentrations of digitoxin, acetyldigitoxin or other solutes as competing agents. A fixed concentration of β-cyclodextrin was also present in the mobile phase as a solubilising agent. It was found that digitoxin and acetyldigitoxin each had strong interactions at a single common binding site on HSA, but with slightly different equilibrium constants for this region. Neither compound showed any competition with warfarin or L-tryptophan, which were used as probes for binding at the warfarin-azapropazone and indole-benzodiazepine sites of HSA. These results confirmed the presence of a separate binding region on HSA for digitoxin-related compounds. Copyright (C) 1999 Elsevier Science B.V.

AB - Zonal elution and high-performance affinity chromatography were used to examine interactions of the drugs digitoxin and acetyldigitoxin with the protein human serum albumin (HSA). This was done by injecting small amounts of digitoxin and acetyldigitoxin onto an immobilized HSA column in the presence of mobile phases that contained various concentrations of digitoxin, acetyldigitoxin or other solutes as competing agents. A fixed concentration of β-cyclodextrin was also present in the mobile phase as a solubilising agent. It was found that digitoxin and acetyldigitoxin each had strong interactions at a single common binding site on HSA, but with slightly different equilibrium constants for this region. Neither compound showed any competition with warfarin or L-tryptophan, which were used as probes for binding at the warfarin-azapropazone and indole-benzodiazepine sites of HSA. These results confirmed the presence of a separate binding region on HSA for digitoxin-related compounds. Copyright (C) 1999 Elsevier Science B.V.

KW - Acetyldigitoxin

KW - Digitoxin

KW - Human serum albumin

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