Binding of amino acids to the cationic surfactant cetyltrimethylammoniumbromide

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Abstract

The interaction of amino acids with the cationic surfactant cetyltrimethylammoniumbromide (CTAB) 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 Arg, Glu, Gly, Leu, Lys, Met, Nle, Phe Trp, Tyr and Val to the surfactant was observed, however, the strength of interaction was fairly low. The hydrophobicity of the amino acid side chains significantly influenced the strength of interaction. The findings support the hypothesis that the binding of cationic surfactants to proteins involves more than one amino acid residues and that the hydrophobic forces have a considerable impact on the interaction.

Original languageEnglish
Pages (from-to)555-562
Number of pages8
JournalBiochemistry and Molecular Biology International
Volume37
Issue number3
Publication statusPublished - 1995

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Cationic surfactants
Surface-Active Agents
Amino Acids
Hydrophobicity
Hydrophobic and Hydrophilic Interactions
Thin layer chromatography
Reverse-Phase Chromatography
Thin Layer Chromatography
Charge transfer
Proteins

ASJC Scopus subject areas

  • Biochemistry
  • Genetics
  • Molecular Biology

Cite this

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abstract = "The interaction of amino acids with the cationic surfactant cetyltrimethylammoniumbromide (CTAB) 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 Arg, Glu, Gly, Leu, Lys, Met, Nle, Phe Trp, Tyr and Val to the surfactant was observed, however, the strength of interaction was fairly low. The hydrophobicity of the amino acid side chains significantly influenced the strength of interaction. The findings support the hypothesis that the binding of cationic surfactants to proteins involves more than one amino acid residues and that the hydrophobic forces have a considerable impact on the interaction.",
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T1 - Binding of amino acids to the cationic surfactant cetyltrimethylammoniumbromide

AU - Cserháti, T.

AU - Forgács, E.

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N2 - The interaction of amino acids with the cationic surfactant cetyltrimethylammoniumbromide (CTAB) 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 Arg, Glu, Gly, Leu, Lys, Met, Nle, Phe Trp, Tyr and Val to the surfactant was observed, however, the strength of interaction was fairly low. The hydrophobicity of the amino acid side chains significantly influenced the strength of interaction. The findings support the hypothesis that the binding of cationic surfactants to proteins involves more than one amino acid residues and that the hydrophobic forces have a considerable impact on the interaction.

AB - The interaction of amino acids with the cationic surfactant cetyltrimethylammoniumbromide (CTAB) 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 Arg, Glu, Gly, Leu, Lys, Met, Nle, Phe Trp, Tyr and Val to the surfactant was observed, however, the strength of interaction was fairly low. The hydrophobicity of the amino acid side chains significantly influenced the strength of interaction. The findings support the hypothesis that the binding of cationic surfactants to proteins involves more than one amino acid residues and that the hydrophobic forces have a considerable impact on the interaction.

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