desHis1Glu9-glucagon

desHis1Glu9-glucagon (also known as des-His1-[Glu9]glucagon amide) is a synthetic peptide analogue of glucagon that acts as a competitive glucagon receptor (GCGR) antagonist. Originally designed and synthesized at Rockefeller University, and later extensively studied by the University of Ulster, the peptide is modified by deleting the histidine residue at position 1 and replacing the aspartic acid at position 9 with glutamic acid. This structural modification renders the peptide highly stable against enzymatic degradation by dipeptidyl peptidase-4 (DPP-4) compared to native glucagon. In vitro, desHis1Glu9-glucagon binds to glucagon receptors and blocks glucagon-induced adenylyl cyclase activation and insulin secretion, while displaying no agonist activity on the adenylyl cyclase pathway. In vivo, it prevents glucagon-induced hyperglycemia and reduces blood glucose levels in animal models of diabetes, making it a valuable research tool and therapeutic candidate for the treatment of type 2 diabetes.

Other names

[des-His1,Glu9]-glucagon (1-29) amide[des-His1,Glu9]-glucagon amidedes-His1-[Glu9]-glucagon (1-29) amidedes-His1-[Glu9]-glucagon amidedes-His1-[Glu9]glucagondes-His1-[Glu9]glucagon amidedes-His1,Glu9-glucagon amidedesHis1Glu9glucagon-amidedesHis-1Glu9glucagon-amidedesHis 1Glu9glucagon-amide