Charge-transfer chromatographic study on the interaction of amino acids with ethoxylated stearic acid surfactants

Research output: Contribution to journalArticle

7 Citations (Scopus)

Abstract

The interaction of amino acids with ethoxylated stearic acid nonionic surfactants was studied by charge-transfer reversed-phase thin-layer chromatography and the relative strength of interaction was calculated. In the majority of cases the surfactant has a negligible effect on the hydrophobicity of amino acids. Only the binding of Asn, Cys, Gln, Leu, Lys, Met, Nle, Phe, Ser, Trp and Tyr to the surfactants was observed, however, the strength of interaction was fairly low. Stepwise regression analysis proved that the electronic parameters of the amino acids have the highest impact on the strength of interaction. This finding supports the hypothesis that the binding of ethoxylated stearic acid nonionic surfactants to proteins involves more than one amino acid residues and that the hydrophilic forces have a considerable impact on the interaction.

Original languageEnglish
Pages (from-to)45-48
Number of pages4
JournalBiomedical Chromatography
Volume8
Issue number1
Publication statusPublished - 1994

Fingerprint

Surface-Active Agents
Charge transfer
Amino Acids
Nonionic surfactants
Thin layer chromatography
Reverse-Phase Chromatography
Hydrophobicity
Thin Layer Chromatography
Hydrophobic and Hydrophilic Interactions
Regression analysis
Regression Analysis
stearic acid
Proteins

ASJC Scopus subject areas

  • Biochemistry, Genetics and Molecular Biology(all)
  • Biochemistry
  • Clinical Biochemistry
  • Analytical Chemistry
  • Pharmacology

Cite this

@article{ca70c06abe3d4140af5b54637882518b,
title = "Charge-transfer chromatographic study on the interaction of amino acids with ethoxylated stearic acid surfactants",
abstract = "The interaction of amino acids with ethoxylated stearic acid nonionic surfactants was studied by charge-transfer reversed-phase thin-layer chromatography and the relative strength of interaction was calculated. In the majority of cases the surfactant has a negligible effect on the hydrophobicity of amino acids. Only the binding of Asn, Cys, Gln, Leu, Lys, Met, Nle, Phe, Ser, Trp and Tyr to the surfactants was observed, however, the strength of interaction was fairly low. Stepwise regression analysis proved that the electronic parameters of the amino acids have the highest impact on the strength of interaction. This finding supports the hypothesis that the binding of ethoxylated stearic acid nonionic surfactants to proteins involves more than one amino acid residues and that the hydrophilic forces have a considerable impact on the interaction.",
author = "T. Cserhati",
year = "1994",
language = "English",
volume = "8",
pages = "45--48",
journal = "Biomedical Chromatography",
issn = "0269-3879",
publisher = "John Wiley and Sons Ltd",
number = "1",

}

TY - JOUR

T1 - Charge-transfer chromatographic study on the interaction of amino acids with ethoxylated stearic acid surfactants

AU - Cserhati, T.

PY - 1994

Y1 - 1994

N2 - The interaction of amino acids with ethoxylated stearic acid nonionic surfactants was studied by charge-transfer reversed-phase thin-layer chromatography and the relative strength of interaction was calculated. In the majority of cases the surfactant has a negligible effect on the hydrophobicity of amino acids. Only the binding of Asn, Cys, Gln, Leu, Lys, Met, Nle, Phe, Ser, Trp and Tyr to the surfactants was observed, however, the strength of interaction was fairly low. Stepwise regression analysis proved that the electronic parameters of the amino acids have the highest impact on the strength of interaction. This finding supports the hypothesis that the binding of ethoxylated stearic acid nonionic surfactants to proteins involves more than one amino acid residues and that the hydrophilic forces have a considerable impact on the interaction.

AB - The interaction of amino acids with ethoxylated stearic acid nonionic surfactants was studied by charge-transfer reversed-phase thin-layer chromatography and the relative strength of interaction was calculated. In the majority of cases the surfactant has a negligible effect on the hydrophobicity of amino acids. Only the binding of Asn, Cys, Gln, Leu, Lys, Met, Nle, Phe, Ser, Trp and Tyr to the surfactants was observed, however, the strength of interaction was fairly low. Stepwise regression analysis proved that the electronic parameters of the amino acids have the highest impact on the strength of interaction. This finding supports the hypothesis that the binding of ethoxylated stearic acid nonionic surfactants to proteins involves more than one amino acid residues and that the hydrophilic forces have a considerable impact on the interaction.

UR - http://www.scopus.com/inward/record.url?scp=0028052998&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0028052998&partnerID=8YFLogxK

M3 - Article

C2 - 8130634

AN - SCOPUS:0028052998

VL - 8

SP - 45

EP - 48

JO - Biomedical Chromatography

JF - Biomedical Chromatography

SN - 0269-3879

IS - 1

ER -