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Norbornene-based anion receptors as D-alanine binders

Long, Benjamin M. and Pfeffer, Frederick M. 2015, Norbornene-based anion receptors as D-alanine binders, Supramolecular chemistry, vol. 27, no. 11-12, Special Issue: Australasian supramolecular chemistry issue, pp. 847-853, doi: 10.1080/10610278.2015.1089999.

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Title Norbornene-based anion receptors as D-alanine binders
Author(s) Long, Benjamin M.ORCID iD for Long, Benjamin M. orcid.org/0000-0002-3248-8851
Pfeffer, Frederick M.ORCID iD for Pfeffer, Frederick M. orcid.org/0000-0002-5441-6437
Journal name Supramolecular chemistry
Volume number 27
Issue number 11-12
Season Special Issue: Australasian supramolecular chemistry issue
Start page 847
End page 853
Total pages 7
Publisher Taylor & Francis
Place of publication London, Eng.
Publication date 2015
ISSN 1061-0278
1029-0478
Keyword(s) Science & Technology
Physical Sciences
Chemistry, Multidisciplinary
Chemistry
anion binding
NMR titration
antibacterial
vancomycin
ALA-D-LAC
GLYCOPEPTIDE ANTIBIOTICS
BINDING
ANALOGS
Summary 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-d6 (Log Ka 1-2 for TBA Acetyl D-Alanine) in the anticipated 1:1 mode of binding.
Language eng
DOI 10.1080/10610278.2015.1089999
Field of Research 030302 Nanochemistry and Supramolecular Chemistry
030503 Organic Chemical Synthesis
03 Chemical Sciences
Socio Economic Objective 970103 Expanding Knowledge in the Chemical Sciences
HERDC Research category C1 Refereed article in a scholarly journal
ERA Research output type C Journal article
Grant ID ARC DP 140100227
Copyright notice ©2015, Taylor & Francis
Persistent URL http://hdl.handle.net/10536/DRO/DU:30080465

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