Norbornene-based anion receptors as D-alanine binders

Abstract

Vancomycin is currently used as last-line therapy against many Gram-positive bacterial pathogens. Herein, we report a series of peptidomimetic norbornene-based anion receptors that were designed as simple vancomycin mimics New hosts were evaluated for their affinity to both acetate and acetyl D-Ala by ¹H NMR titration. Modest binding to both anions was observed in DMSO-d ₆ (Log K_a 1–2 for TBA Acetyl D-Alanine) in the anticipated 1:1 mode of binding.

Keywords:

• anion binding
• NMR titration
• antibacterial
• vancomycin

Supplemental data

Supplemental data for this article can be accessed here: http://dx.doi.org/10.1080/10610278.2015.1086764.

Acknowledgements

The authors would like to thank Professors Roger Nation and Jian Li for assistance with the disk diffusion assay and Dr Deni Taleski for his insight.

Notes

1. While the modified Job Plots did not contibute reliable data for assesment of binding stoiciometry, in this study, they are included in the supplemental data for full disclosure of results.