Glucagon-like peptide-1 (GLP-1) is an incretin hormone primarily produced in the intestinal L-cells in response to food intake. It is a 30-amino acid peptide derived from the proglucagon gene and exists in several forms, with GLP-1(7-36)amide being the most biologically active. Researchers have synthesized GLP-1 analogs to enhance its stability and therapeutic potential, given its rapid degradation by the enzyme dipeptidyl peptidase-4 (DPP-4). GLP-1 is a significant focus in metabolic research due to its role in glucose homeostasis and appetite regulation. Researchers have observed that GLP-1 enhances insulin secretion in a glucose-dependent manner, inhibits glucagon release, and slows gastric emptying, contributing to its potential in managing type 2 diabetes and obesity. Additionally, GLP-1 has been investigated for its neuroprotective effects and potential benefits in cardiovascular health. The mechanism of action of GLP-1 involves binding to the GLP-1 receptor, a G-protein-coupled receptor, which activates adenylate cyclase and increases cyclic AMP levels, leading to insulin secretion and other downstream effects. Pharmacokinetically, GLP-1 has a short half-life of approximately 1-2 minutes due to rapid enzymatic degradation, necessitating the development of longer-acting analogs for therapeutic use. The bioavailability of GLP-1 is poor when administered orally, thus it is typically delivered via injection. Current research on GLP-1 focuses on developing stable analogs and exploring its broader therapeutic applications. In terms of regulatory status, GLP-1 analogs are approved for use in managing type 2 diabetes in several countries, though the native peptide itself is not used therapeutically due to its instability.