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The glucagon receptor antagonist BI‐32169 constitutes a new class of lasso peptides
Author(s) -
Knappe Thomas A.,
Linne Uwe,
Xie Xiulan,
Marahiel Mohamed A.
Publication year - 2010
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2009.12.046
Subject(s) - peptide , antagonist , lasso (programming language) , chemistry , class (philosophy) , receptor , computational biology , biochemistry , biology , computer science , artificial intelligence , world wide web
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‐32169.