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Domain requirement of moenomycin binding to bifunctional transglycosylases and development of high-throughput discovery of antibiotics

Academic Article
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Overview

authors

  • Cheng, T. J. R.
  • Sung, M. T.
  • Liao, H. Y.
  • Chang, Y. F.
  • Chen, C. W.
  • Huang, C. Y.
  • Chou, L. Y.
  • Wu, Y. D.
  • Chen, Y.
  • Cheng, Y. S. E.
  • Wong, Chi-Huey
  • Ma, C.
  • Cheng, W. C.

publication date

  • January 2008

journal

  • Proceedings of the National Academy of Sciences of the United States of America  Journal

abstract

  • Moenomycin inhibits bacterial growth by blocking the transglycosylase activity of class A penicillin-binding proteins (PBPs), which are key enzymes in bacterial cell wall synthesis. We compared the binding affinities of moenomycin A with various truncated PBPs by using surface plasmon resonance analysis and found that the transmembrane domain is important for moenomycin binding. Full-length class A PBPs from 16 bacterial species were produced, and their binding activities showed a correlation with the antimicrobial activity of moenomycin against Enterococcus faecalis and Staphylococcus aureus. On the basis of these findings, a fluorescence anisotropy-based high-throughput assay was developed and used successfully for identification of transglycosylase inhibitors.

subject areas

  • Anisotropy
  • Cell Wall
  • Chemistry, Pharmaceutical
  • Drug Design
  • Enterococcus faecalis
  • Glycosyltransferases
  • Inhibitory Concentration 50
  • Kinetics
  • Models, Chemical
  • Oligosaccharides
  • Penicillin-Binding Proteins
  • Spectrometry, Fluorescence
  • Staphylococcus aureus
  • Surface Plasmon Resonance
  • Technology, Pharmaceutical
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Research

keywords

  • fluorescence anisotropy
  • penicillin-binding proteins
  • transglycosylase inhibitors
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Identity

PubMed Central ID

  • PMC2206553

International Standard Serial Number (ISSN)

  • 0027-8424

Digital Object Identifier (DOI)

  • 10.1073/pnas.0710868105

PubMed ID

  • 18182485
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Additional Document Info

start page

  • 431

end page

  • 436

volume

  • 105

issue

  • 2

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