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 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.
Knappe
Thomas A
TA
Department of Chemistry/Biochemistry, Philipps-University Marburg, Marburg, Germany.
Linne
Uwe
U
Xie
Xiulan
X
Marahiel
Mohamed A
MA
D000595:Amino Acid Sequence; D001426:Bacterial Proteins / Q000737:chemistry / Q000235:genetics / Q000494:pharmacology; D002851:Chromatography, High Pressure Liquid; D009682:Magnetic Resonance Spectroscopy; D008958:Models, Molecular; D008969:Molecular Sequence Data; D010456:Peptides, Cyclic / Q000737:chemistry* / Q000235:genetics / Q000494:pharmacology*; D011487:Protein Conformation; D017510:Protein Folding; D018027:Receptors, Glucagon / Q000037:antagonists & inhibitors*; D013302:Streptomyces / Q000378:metabolism; D053719:Tandem Mass Spectrometry / Q000379:methods
C493079:BI-32169; D001426:Bacterial Proteins; D010456:Peptides, Cyclic; D018027:Receptors, Glucagon