Binding of amino acids and peptides to bovine serum albumin studied by charge transfer chromatography

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2 Citations (Scopus)

Abstract

The interaction of 12 amino acids and peptides with bovine serum albumin was studied by charge-transfer reversed-phase thin-layer chromatography and the relative strength of interaction was calculated. Ala, Leu, Phe and Met-Tyr interacted with the bovine serum albumin showing considerable differences in the binding strength. Stepwise regression analysis proved that the bulkiness of the side chain of solutes exert a significant impact on their capacity to bind to serum albumin. This result supports the hypothesis that the sterical correspondence between the side chain of solutes and the binding site of the surface of albumin molecule governs the interaction.

Original languageEnglish
Pages (from-to)11-16
Number of pages6
JournalInternational Journal of Bio-Chromatography
Volume5
Issue number1
Publication statusPublished - 2000

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Bovine Serum Albumin
Chromatography
Charge transfer
Amino Acids
Thin layer chromatography
Peptides
Reverse-Phase Chromatography
Thin Layer Chromatography
Regression analysis
Serum Albumin
Albumins
Binding Sites
Regression Analysis
Molecules

Keywords

  • Amino acid and peptide binding
  • Bovine serum albumin
  • Charge transfer chromatography

ASJC Scopus subject areas

  • Biochemistry

Cite this

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AU - Forgács, E.

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AB - The interaction of 12 amino acids and peptides with bovine serum albumin was studied by charge-transfer reversed-phase thin-layer chromatography and the relative strength of interaction was calculated. Ala, Leu, Phe and Met-Tyr interacted with the bovine serum albumin showing considerable differences in the binding strength. Stepwise regression analysis proved that the bulkiness of the side chain of solutes exert a significant impact on their capacity to bind to serum albumin. This result supports the hypothesis that the sterical correspondence between the side chain of solutes and the binding site of the surface of albumin molecule governs the interaction.

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