4.8 Article

Design of Monodisperse and Well-Defined Polypeptide-Based Polyvalent Inhibitors of Anthrax Toxin

期刊

ANGEWANDTE CHEMIE-INTERNATIONAL EDITION
卷 53, 期 31, 页码 8037-8040

出版社

WILEY-V C H VERLAG GMBH
DOI: 10.1002/anie.201400870

关键词

anthrax toxin; multivalency; periodic polypeptides; protein engineering; structure-activity relationships

资金

  1. NIH [U01 AI056546, R01 EB015482]
  2. P. K. Lashmet Chair Fund

向作者/读者索取更多资源

The design of polyvalent molecules, presenting multiple copies of a specific ligand, represents a promising strategy to inhibit pathogens and toxins. The ability to control independently the valency and the spacing between ligands would be valuable for elucidating structure-activity relationships and for designing potent polyvalent molecules. To that end, we designed monodisperse polypeptide-based polyvalent inhibitors of anthrax toxin in which multiple copies of an inhibitory toxin-binding peptide were separated by flexible peptide linkers. By tuning the valency and linker length, we designed polyvalent inhibitors that were over four orders of magnitude more potent than the corresponding monovalent ligands. This strategy for the rational design of monodisperse polyvalent molecules may not only be broadly applicable for the inhibition of toxins and pathogens, but also for controlling the nanoscale organization of cellular receptors to regulate signaling and the fate of stem cells.

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