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Binding of a dimeric derivative of vancomycin to l-Lys-d-Ala- d-lactate in solution and at a surface by Jianghong Rao; Lin Yan; Joydeep Lahiri; George M Whitesides; Robert M Weis; H Shaw Warren is a Biochemistry, Genetics and Molecular Biology article available to read on EtoBox.

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## Background: The emergence of bacteria that are resistant to vancomycin (V), a glyeopeptide antibiotic, results from the replacement of the carboxy-terminal D-Ala-D-Ala of bacterial cell wall precursors by D-Ala-D-lactate. Recently, it has been demonstrated that covalent dimeric variants of V are active against vancomycin-resistant enterococci (VRE). To study the contribution of divalency to the activities of these variants, we modeled the interactions of V and a dimeric V with L-Lys-D-Ala-D-lactate, an analog of the cell-wall precursors of the vancomycin-resistant bacteria. Results: A dimeric derivative of V (V-Rd-V) was found to be much more effective than V in inhibiting the growth of VRE. The interactions of V and V-Rd-V with a monomeric lactate ligand --diaeetyI-L-Lys-o-Ala-D-lactate (Ac2KDADLac) --and a dimeric derivative of L-Lys-D-Ala-D-lactate (Lac-R'd-Lac) in solution have been examined using isothermal titration calorimetry and UV spectroscopy titrations; the results reveal that V-Rd-V binds Lac-R'd-Lac approximately 40 times more tightly than V binds Ac2KDADLac. Binding of V and of V-Rd-V to/V~-Ac-L-Lys-D-Ala-D-lactate presented on the surface of mixed self-assembled

Who reads Binding of a dimeric derivative of vancomycin to l-Lys-d-Ala- d-lactate in solution and at a surface?

Author

Jianghong Rao; Lin Yan; Joydeep Lahiri; George M Whitesides; Robert M Weis; H Shaw Warren

Publisher

Elsevier Science; Elsevier ; Cell Press; Elsevier BV (ISSN 1074-5521)

Published

1999

Language

EN

Field

Biochemistry, Genetics and Molecular Biology (Life Sciences)