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PMID: 20043911 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't

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

FEBS letters ·Vol. 584 ·No. 4 ·2010-02-19 ·Pages 785-9

Knappe TA, Linne U, Xie X, Marahiel MA

Abstract

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.

MeSH Terms
Amino Acid Sequence Bacterial Proteins/chemistry,genetics,pharmacology Chromatography, High Pressure Liquid Magnetic Resonance Spectroscopy Models, Molecular Molecular Sequence Data Peptides, Cyclic/chemistry,genetics,pharmacology Protein Conformation Protein Folding Receptors, Glucagon/antagonists & inhibitors Streptomyces/metabolism Tandem Mass Spectrometry/methods
Chemicals
BI-32169 Bacterial Proteins Peptides, Cyclic Receptors, Glucagon
Authors & Affiliations
4 authors, click to expand affiliations / ORCID
Knappe Thomas A
Department of Chemistry/Biochemistry, Philipps-University Marburg, Marburg, Germany.
Linne Uwe
Xie Xiulan
Marahiel Mohamed A
Article Info
Journal
FEBS letters
Abbr.
FEBS Lett
ISSN
1873-3468
Published
2010-02-19
Epub
2009-00-30
Pages
785-9
Language
English
Region
England
NLM ID
0155157
Subset
IM
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