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.

Binding of Dipeptides and Amino Acids to Teicoplanin Chiral Stationary Phase: Apparent Homogeneity of Some Heterogeneous Systems / Alberto, Cavazzini; Luisa, Pasti; Francesco, Dondi; Marco, Finessi; Valentina, Costa; Gasparrini, Francesco; F., Bedani; Ciogli, Alessia. - In: ANALYTICAL CHEMISTRY. - ISSN 0003-2700. - 81:16(2009), pp. 6735-6743. [10.1021/ac900677f]

Binding of Dipeptides and Amino Acids to Teicoplanin Chiral Stationary Phase: Apparent Homogeneity of Some Heterogeneous Systems

GASPARRINI, Francesco;CIOGLI, Alessia
2009

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.
2009
01 Pubblicazione su rivista::01a Articolo in rivista
Binding of Dipeptides and Amino Acids to Teicoplanin Chiral Stationary Phase: Apparent Homogeneity of Some Heterogeneous Systems / Alberto, Cavazzini; Luisa, Pasti; Francesco, Dondi; Marco, Finessi; Valentina, Costa; Gasparrini, Francesco; F., Bedani; Ciogli, Alessia. - In: ANALYTICAL CHEMISTRY. - ISSN 0003-2700. - 81:16(2009), pp. 6735-6743. [10.1021/ac900677f]
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Utilizza questo identificativo per citare o creare un link a questo documento: https://hdl.handle.net/11573/134652
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