This work was supported by the National Science Council and Academia Sinica.
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Communication
Effect of the Peptide Moiety of Lipid II on Bacterial Transglycosylase†
Article first published online: 5 SEP 2012
DOI: 10.1002/anie.201204038
Copyright © 2012 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim
Issue
1521-3773/asset/cover.gif?v=1&s=412bc65bdcb3f0e34a94f27c1c13e908726694d4 "Angewandte Chemie International Edition")
Angewandte Chemie International Edition
Volume 51, Issue 40, pages 10123–10126, October 1, 2012
Additional Information
How to Cite
Shih, H.-W., Chang, Y.-F., Li, W.-J., Meng, F.-C., Huang, C.-Y., Ma, C., Cheng, T.-J. R., Wong, C.-H. and Cheng, W.-C. (2012), Effect of the Peptide Moiety of Lipid II on Bacterial Transglycosylase . Angew. Chem. Int. Ed., 51: 10123–10126. doi: 10.1002/anie.201204038
- †
Publication History
- Issue published online: 26 SEP 2012
- Article first published online: 5 SEP 2012
- Manuscript Received: 24 MAY 2012
Funded by
- National Science Council
- Academia Sinica
Keywords:
- antibiotics;
- biological activity;
- carbohydrates;
- natural products;
- structure-activity relationships
The writing's on the (cell) wall: A series of Lipid II analogues with modifications to the peptide moiety were evaluated as substrates of bacterial transglycosylase. The first two positions on the peptide, D-lactate and L-alanine (see scheme), especially their methyl groups, were found to be essential for substrate-binding activity, an important discovery for the design of antibiotics to inhibit cell-wall biosynthesis.