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

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...

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Veröffentlicht in:	FEBS letters 2010-02, Vol.584 (4), p.785-789
Hauptverfasser:	Knappe, Thomas A., Linne, Uwe, Xie, Xiulan, Marahiel, Mohamed A.
Format:	Artikel
Sprache:	eng
Schlagworte:	Amino Acid Sequence Bacterial Proteins - chemistry Bacterial Proteins - genetics Bacterial Proteins - pharmacology Chromatography, High Pressure Liquid Disulfide bond formation Glucagon receptor antagonist Lasso peptide Magnetic Resonance Spectroscopy Mass fragmentation Models, Molecular Molecular Sequence Data NMR structure Peptides, Cyclic - chemistry Peptides, Cyclic - genetics Peptides, Cyclic - pharmacology Protein Conformation Protein Folding Protein scaffold Receptors, Glucagon - antagonists & inhibitors Streptomyces Streptomyces - metabolism Tandem Mass Spectrometry - methods
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Zusammenfassung:	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.
ISSN:	0014-5793 1873-3468
DOI:	10.1016/j.febslet.2009.12.046