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Glucose-dependent insulinotropic polypeptide [1-30], commonly referred to as GIP(1-30), is a truncated, bioactive fragment of the endogenous 42-amino acid incretin hormone GIP. Produced by K-cells in the small intestine, this peptide functions as a potent agonist of the GIP receptor (GIPR). It retains the full insulinotropic potency of the native hormone, stimulating insulin secretion from pancreatic beta cells in a glucose-dependent manner. The amidated form, GIP(1-30)NH2, is the most biologically relevant truncated version and has been extensively studied in clinical research. While it plays a significant role in the 'incretin effect,' the native peptide is rapidly degraded by the enzyme dipeptidyl peptidase-4 (DPP-4), resulting in a very short circulating half-life. It has been investigated in early-stage clinical trials for its potential therapeutic application in type 2 diabetes and metabolic disorders, although its rapid clearance often requires stabilized analogues or continuous infusion for sustained effect.
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