Journal of Natural Products · 2004 · 75 citations · 9 references
PharmacyBiochemistryPharmacologyDrug DiscoveryStructural BiologyStructure-activity RelationshipsPeptide AnalysisPeptide ChemistryPeptide Drug DiscoveryAmino Acid AnalysisAmino Acid Composition AnalysisAmino AcidsDisulfide Bond StructureGlucagon Receptor AntagonismGlucagon Receptor PharmacologyPeptide Mass SpectrometryPeptide Structure-activity Relationships
A new bicyclic 19-peptide, BI-32169, has been isolated from the culture broth of Streptomyces sp. (DSM 14996). Its structure has been established by amino acid analysis, mass spectrometry, and 2D NMR analysis. BI-32169 consists exclusively of protein amino acids and is cyclized from the side chain of Asp(9) to the N-terminus of Gly(1). One disulfide bond between Cys(6) and Cys(19) forms a bicyclic structure. BI-32169 and its methyl ester derivative showed potent inhibitory activity against the human glucagon receptor (IC(50) 440 and 320 nM, respectively) in a functional cell-based assay.
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Effects of skyrin, a receptor-selective glucagon antagonist, in rat and human hepatocytes.
Jeremy C. Parker, R. Kirk McPherson, Kim Andrews et al. · Diabetes · 2000 · 65 citations · Full text