esculentin-2CHa(1-30)

Esculentin-2CHa(1-30) is a synthetic linear peptide derived from the N-terminal 30 amino acids of esculentin-2CHa, an antimicrobial peptide found in the skin of amphibians such as *Rana chiricahuensis*. It lacks the cyclic C-terminal domain (CKISKQC) seen in the full-length 37-amino acid esculentin-2CHa. Esculentin-2CHa(1-30) and its analogues have demonstrated broad-spectrum antimicrobial activity, low toxicity toward mammalian cells, and potent insulinotropic/anti-hyperglycemic effects in preclinical models. The peptide stimulates insulin release from pancreatic β-cells by mechanisms including membrane depolarization, increased intracellular calcium, and likely involvement of K_ATP channel closure and voltage-dependent Ca^2+^ channel activation. In mouse models, esculentin-2CHa(1-30) analogues have been shown to improve glucose tolerance and enhance insulin secretion, supporting preclinical potential for type 2 diabetes and related metabolic disorders such as obesity and non-alcoholic fatty liver disease. Recent work includes engineered long-acting fusion protein forms to prolong plasma half-life and enhance in vivo efficacy[3][5][6].

Other names

esc(1-30)