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Dipeptidyl peptidase 4 (DPP-4) inhibitors block a serine protease that trims dipeptides from incretin hormones. DPP-4, also known as cluster of differentiation 26 (CD26), prefers substrates with proline or alanine at the second position. In 1993 it was shown to cleave glucagon-like peptide-1 (GLP-1) and gastric inhibitory polypeptide (GIP) and to account for their degradation in human serum. Inhibiting the enzyme therefore prolongs incretin signaling in studies of glucose homeostasis and insulin secretion. Sitagliptin, alogliptin benzoate and linagliptin bind to the active site without forming a covalent bond. Vildagliptin and saxagliptin are cyanopyrrolidines that form a reversible covalent adduct with the catalytic serine. Trelagliptin and gemigliptin add further gliptin scaffolds for structure-activity comparisons.
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.
Lys-Ala-pNA is a hydrolytic substrate specifically designed for dipeptidyl peptidase II (DPP II). Exhibiting a Michaelis constant (Km) of 0.42 mM, it serves as an effective tool for studying DPP II activity. This substrate is valuable in researching metabolic disorders and understanding DPP II's role in various physiological processes.
