Reversible binding interactions between the tryptophan enantiomers and albumins of different animal species as determined by novel high performance liquid chromatographic methods: an attempt to localize the D- and L-tryptophan binding sites on the human serum albumin polypeptide chain by using protein fragments

Reviews devoted to drug-protein binding present mostly a variety of analytical methods applied to studying the unique process when the protein reversibly binds a low-molecular-weight substance-the drug. This report, however, reviews the great majority of papers presenting the application of one particular method introduced by Hummel and Dreyer in 1962: Measurement of protein-binding phenomena by gel filtration. The main criterion in reviewing published papers was the application of the Hummel-Dreyer method when the counterpart substances were the drug and the human plasma protein.

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Chiral resolution of tryptophan derivatives by CE using canine serum albumin and bovine serum albumin as chiral selectors

Hödl

Koidl

Schmid

2006

Electrophoresis

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This work deals with the application of BSA and canine serum albumin (CSA) for enantioseparation of tryptophan derivatives with CE. The aim of this work was the investigation of the influence of different functional groups of tryptophan derivatives on enantioseparation. CSA as a chiral selector was tested to compare its selector properties with those of BSA. The enantiomers of the tryptophan derivatives were separated by adding BSA or CSA to the BGE. The influence of pH, temperature, BSA and CSA concentration and organic modifiers was investigated. It was found that the stereoselectivity for the different tryptophan derivatives is dependent on the albumin species. It turned out that the different functional groups of the derivatives showed a significant influence on stereoselectivity.

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Cited by 13 publications

References 15 publications

A new approach to human serum albumin chiral stationary phase synthesis and its use in capillary liquid chromatography and capillary electrochromatography

A new approach to human serum albumin chiral stationary phase synthesis and its use in capillary liquid chromatography and capillary electrochromatography

The Hummel–Dreyer method: impact in pharmacology

Chiral resolution of tryptophan derivatives by CE using canine serum albumin and bovine serum albumin as chiral selectors

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