The glucagon receptor antagonist BI‐32169 constitutes a new class of lasso peptides

  title={The glucagon receptor antagonist BI‐32169 constitutes a new class of lasso peptides},
  author={T. Knappe and U. Linne and X. Xie and M. Marahiel},
  journal={FEBS Letters},
  • T. Knappe, U. Linne, +1 author M. Marahiel
  • Published 2010
  • Medicine, Chemistry
  • FEBS Letters
  • The glucagon receptor antagonist BI‐32169, recently isolated from Streptomyces sp., was described as a bicyclic peptide, although its primary structure comprises conserved elements of class I and class II lasso peptides. Tandem mass spectrometric and nuclear magnetic resonance spectroscopic studies revealed that BI‐32169 is a lasso‐structured peptide constituting the new class III of lasso peptides. The determined lasso fold opens new avenues to improve the promising biological activity of BI… CONTINUE READING

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    Publications referenced by this paper.
    BI-32169, a bicyclic 19-peptide with strong glucagon receptor antagonist activity from Streptomyces sp.
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    Insights into the biosynthesis and stability of the lasso peptide capistruin.
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    Structure of microcin J25, a peptide inhibitor of bacterial RNA polymerase, is a lassoed tail.
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