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  • Title: Binding of dipeptides and amino acids to Teicoplanin chiral stationary phase: apparent homogeneity of some heterogeneous systems.
    Author: Cavazzini A, Pasti L, Dondi F, Finessi M, Costa V, Gasparrini F, Ciogli A, Bedani F.
    Journal: Anal Chem; 2009 Aug 15; 81(16):6735-43. PubMed ID: 19630419.
    Abstract:
    The binding between Teicoplanin glycopeptide antibiotic and some dipeptides and amino acids has been studied by nonlinear liquid chromatography. A Teicoplanin-based chiral stationary phase, specifically designed to achieve maximum selectivity and loading by reducing non-specific interactions, has been prepared and packed into a microbore column. The adsorption isotherms of the enantiomers of proline, alanine, and alanine-alanine (Ala-Ala) have been measured through frontal analysis. The experimental binding data have been interpreted in the context of the ordinary homogeneous Michaelis-Menten model and by considering an heterogeneous model that accounts for a broad adsorption energy distribution (AED). AED has been achieved by the analysis of adsorption isotherms. Besides confirming the importance of the terminal D-Ala-D-Ala moiety in the molecular recognition between the dipeptide and the macrocyclic antibiotic Teicoplanin (it was found that Teicoplanin behaves as a molecular filter toward the enantiomers of Ala-Ala), this study shows that a heterogeneous adsorption model is needed for the correct interpretation of binding data.
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