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GLP-1 receptor agonists and modulators act on the receptor for glucagon-like peptide 1 (GLP-1), an incretin hormone. Intestinal L cells release GLP-1 after a meal, and the hormone enhances glucose-dependent insulin secretion from pancreatic beta cells. The receptor, a class B G protein-coupled receptor, was cloned from beta cells by expression cloning in 1992. Peptide agonists in this category include liraglutide and lixisenatide, while tirzepatide also acts at the glucose-dependent insulinotropic polypeptide (GIP) receptor. BETP is a small-molecule ligand that binds the GLP-1 receptor outside the peptide site. The set also includes dipeptidyl peptidase 4 (DPP-4) inhibitors such as linagliptin, which slow the breakdown of endogenous GLP-1.
HAEGT is the first N-terminal 1-5 residues of glucagon like peptide-1 (GLP-1) peptide, and the sequence is His-Ala-Glu-Gly-Thr. HAEGT acts as a competitive substrate for probing prime substrate binding sites of human dipeptidyl peptidase-IV (DPP-IV) 1, in which the N-terminal His-Ala is catalyzed cleavage by DPP-IV. HAEGT can be used in the research of diabetes, obesity.
