5905-41-9Relevant articles and documents
Synthesis and shift-reagent-assisted full NMR assignment of bacterial (: Z 8, e 2,ω)-undecaprenol
Lee, Mijoon,Hesek, Dusan,Zají?ek, Jaroslav,Fisher, Jed F.,Mobashery, Shahriar
, p. 12774 - 12777 (2017/12/06)
The repeating isoprene unit is a fundamental biosynthetic motif. The repetitive structure presents challenges both for synthesis and for structural characterization. In this synthesis of the (Z8,E2,ω)-undecaprenol of prokaryotic glycobiology, we exemplify solutions to these challenges. Allylation of sulfone-derived carbanions controlled the stereochemistry, and its proof-of-structure was secured by Eu(hfc)3 complexation to disperse the overlaid resonances of its 1H NMR spectrum.
Synthesis of a comprehensive polyprenol library for the evaluation of bacterial enzyme lipid substrate specificity
Wu, Baolin,Woodward, Robert,Wen, Liuqing,Wang, Xuan,Zhao, Guohui,Wang, Peng George
, p. 8162 - 8173 (2014/01/06)
Polyprenols, a universal class of glycan-carrier lipids, play important roles in glycan biosynthesis in wide variety of living organisms. The chemical synthesis of natural polyisoprenols such as undecaprenol and dolichols, and even more so the synthesis o
Modular synthesis of diphospholipid oligosaccharide fragments of the bacterial cell wall and their use to study the mechanism of moenomycin and other antibiotics
Gampe, Christian M.,Tsukamoto, Hirokazu,Wang, Tsung-Shing Andrew,Walker, Suzanne,Kahne, Daniel
, p. 9771 - 9778 (2012/02/15)
We present a flexible, modular route to GlcNAc-MurNAc-oligosaccharides that can be readily converted into peptidoglycan (PG) fragments to serve as reagents for the study of bacterial enzymes that are targets for antibiotics. Demonstrating the utility of these synthetic PG substrates, we show that the tetrasaccharide substrate lipid IV (3), but not the disaccharide substrate lipid II (2), significantly increases the concentration of moenomycin A required to inhibit a prototypical PG-glycosyltransferase (PGT). These results imply that lipid IV and moenomycin A bind to the same site on the enzyme. We also show the moenomycin A inhibits the formation of elongated polysaccharide product but does not affect length distribution. We conclude that moenomycin A blocks PG-strand initiation rather than elongation or chain termination. Synthetic access to diphospholipid oligosaccharides will enable further studies of bacterial cell wall synthesis with the long-term goal of identifying novel antibiotics.
