Semaglutide is a recombinant DNA produced polypeptide analog of human glucagon-like peptide-1 (GLP-1) which is used in combination with diet and exercise in the therapy of type 2 diabetes, either alone or in combination with other antidiabetic agents.
CAT No: R1847
CAS No:910463-68-2
Synonyms/Alias:Semaglutide;Rybelsus;Ozempic;910463-68-2;Wegovy;NN9535;UNII-53AXN4NNHX;NN 9535;NNC 0113-0217;53AXN4NNHX;NN-9535;Rybelsus (oral semaglutide);Ozempic (injectable semaglutide);CHEBI:167574;NNC-0113-0217;Semaglutide [USAN:INN];semaglutida;semaglutidum;Oral Semaglutide;Semaglutide free base;Semaglutide(sodium salt)?;GTPL9724;A10BJ06;DTXSID101027903;EX-A2424;AC-32580;FS171058;NNC0480 0389;NN1535 ICOSEMA COMPONENT SEMAGLUTIDE;NN1535 LAISEMA COMPONENT SEMAGLUTIDE;SEMAGLUTIDE COMPONENT OF NN1535 ICOSEMA;Rybelsus;Ozempic;NN9535;OG217SC;NNC 0113-0217;
Sermaglutide is a synthetic peptide analog of human glucagon-like peptide-1 (GLP-1), designed to closely mimic the endogenous incretin hormone involved in glucose homeostasis. As a member of the GLP-1 receptor agonist family, this peptide is structurally modified to enhance stability and prolong biological activity, making it a valuable tool in metabolic research. Its molecular features, including resistance to dipeptidyl peptidase-4 (DPP-4) degradation, allow for extended action in relevant biochemical systems. The functional properties of sermaglutide have positioned it as a prominent research reagent for studying incretin pathways, peptide receptor interactions, and signaling mechanisms that underpin metabolic regulation.
Metabolic pathway elucidation: Researchers utilize sermaglutide to probe the complex signaling networks governing glucose metabolism and energy balance. Its high affinity for GLP-1 receptors enables precise modulation of downstream pathways, allowing scientists to dissect the roles of cyclic AMP production, insulin secretion, and glucagon suppression in cellular and organismal models. Experimental use of this peptide supports mechanistic investigations into how incretin mimetics influence hepatic glucose output, pancreatic beta-cell function, and systemic metabolic responses.
Peptide-receptor interaction studies: The well-characterized structure of sermaglutide makes it a preferred ligand for in vitro and in vivo assays exploring GLP-1 receptor pharmacology. By facilitating receptor binding assays, signal transduction analysis, and structure-activity relationship research, this compound enables detailed characterization of receptor activation kinetics, binding affinities, and downstream effector engagement. Such studies are instrumental in advancing understanding of peptide hormone-receptor dynamics and optimizing ligand design for future research applications.
Pharmacokinetic modeling: Due to its enhanced resistance to enzymatic degradation and prolonged half-life relative to native GLP-1, sermaglutide is widely used in pharmacokinetic and biodistribution studies. Researchers employ this peptide to model absorption, distribution, metabolism, and excretion (ADME) profiles in preclinical systems, yielding critical data for the optimization of peptide-based delivery strategies. These investigations provide insights into the molecular determinants of peptide stability, tissue targeting, and systemic exposure.
Analytical method development: The unique physicochemical properties of sermaglutide render it an effective standard or reference compound in the development and validation of analytical techniques. Laboratories leverage this peptide in high-performance liquid chromatography (HPLC), mass spectrometry, and immunoassay platforms to establish sensitivity, specificity, and reproducibility in peptide quantification protocols. Such applications are essential for ensuring the accuracy and reliability of peptide detection in complex biological matrices.
Peptide synthesis and formulation research: As a chemically defined GLP-1 analog, sermaglutide serves as a model substrate for optimizing solid-phase peptide synthesis, purification, and formulation processes. Its complex structure and sequence modifications present valuable challenges for synthetic methodology development, enabling researchers to refine strategies for peptide assembly, folding, and stabilization. Studies in this area contribute to advances in large-scale peptide manufacturing, formulation stability, and delivery technology relevant to the broader peptide therapeutics field.
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