Partial-filling affinity capillary electrophoresis techniques to probe the binding of glycopeptide antibiotics to D-Ala-D-Ala terminus peptides.

Abstract

This work is an overview of our use of affinity capillary electrophoresis (ACE) to estimate binding constants between D-Ala-D-Ala terminus peptides and the glycopeptides vancomycin (Van) from Streptomyces orientalis, teicoplanin (Teic) from Actinoplanes teicomyceticus, and ristocetin A (Rist) from Nocardia lurida. In these studies, modifications in the ACE technique, including partial-filling ACE (PFACE), flow-through PFACE (FTPFACE), on-column ligand derivatization ACE (OCLDACE), on-column receptor derivatization ACE (OCRDACE), multiple-step ligand injection PFACE (MSLIPFACE), and multiple-injection ACE (MIACE), are described and used to determine binding constants of peptides to antibiotics. The findings described herein demonstrate the advantages of ACE in estimating binding parameters between antibiotics and small peptides over other analytical techniques.

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Cite this paper

@article{Zavaleta2006PartialfillingAC, title={Partial-filling affinity capillary electrophoresis techniques to probe the binding of glycopeptide antibiotics to D-Ala-D-Ala terminus peptides.}, author={J . Orme - Zavaleta and Dinora B Chinchilla and Catherine F Kaddis and Karla Lizeth Sanchez Martinez and Abby Brown and {\'A}lvaro G{\'o}mez and Amaris Pao and Alejandra Ram{\'i}rez and Sanjay M. Nilapwar and John E. Ladbury and Frank A. Gomez}, journal={Journal of capillary electrophoresis and microchip technology}, year={2006}, volume={9 5-6}, pages={101-17} }