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

T. Cserháti, E. Forgács, Zdenek Deyl, Ivan Mikšík

Research output: Contribution to journalArticle

9 Citations (Scopus)

Abstract

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
Volume753
Issue number1
DOIs
Publication statusPublished - Mar 25 2001

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Albumins
Derivatives
Serum Albumin
Thin layer chromatography
Bovine Serum Albumin
Regression analysis
Charge transfer
phenoxyacetic acid
Amino Acids

Keywords

  • Albumin
  • Derivatization, TLC
  • Phenoxyacetic acid

ASJC Scopus subject areas

  • Chemistry(all)

Cite this

Effect of molecular parameters on the binding of phenoxyacetic acid derivatives to albumins. / Cserháti, T.; Forgács, E.; Deyl, Zdenek; Mikšík, Ivan.

In: Journal of Chromatography B: Biomedical Sciences and Applications, Vol. 753, No. 1, 25.03.2001, p. 87-92.

Research output: Contribution to journalArticle

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