Effect of molecular parameters on the binding of phenoxyacetic acid derivatives to albumins

Tibor Cserháti, Esther Forgács, Zdenek Deyl, Ivan Mikšík

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The interaction of 12 phenoxyacetic acid derivatives with human and serum albumin as well as with egg albumin was studied by charge-transfer reversed-phase (RP) thin-layer chromatography (TLC) and the relative strength of interaction was calculated. Each phenoxyacetic acid derivative interacted with human and bovine serum albumins whereas no interaction was observed with egg albumin. Stepwise regression analysis proved that the lipophilicity of the derivatives exert a significant impact on their capacity to bind to serum albumins. This result supports the hypothesis that the binding of phenoxyacetic acid derivatives to albumins may involve hydrophobic forces occurring between the corresponding apolar substructures of these derivatives and the amino acid side chains.

Original languageEnglish
Pages (from-to)87-92
Number of pages6
JournalJournal of Chromatography B: Biomedical Sciences and Applications
Issue number1
Publication statusPublished - Mar 25 2001



  • Albumin
  • Derivatization, TLC
  • Phenoxyacetic acid

ASJC Scopus subject areas

  • Chemistry(all)

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