SEMA
SEMA (Incretin Receptor Agonist)
At a Glance
Molecular Properties
Overview
Compound Description
SEMA is a synthetic 31-amino-acid peptide analog of a naturally occurring human incretin hormone that has been one of the most extensively studied incretin-based research compounds. The molecule features a substitution of alanine to alpha-aminoisobutyric acid (Aib) at position 8 for dipeptidyl peptidase-4 (DPP-4) resistance, and acylation of lysine at position 26 with a C18 fatty diacid chain that enables non-covalent albumin binding. These modifications extend the half-life to approximately 7 days. It is supplied as a characterized reference compound for in-vitro receptor-pharmacology and analytical method development, and is not for human or animal use.
Mechanism of Action
Research-Identified Pathways
SEMA binds to and activates its target incretin receptor, a G-protein-coupled receptor expressed in pancreatic beta cells, the gastrointestinal tract, and specific brain regions including the hypothalamus and hindbrain. Receptor activation initiates cAMP-mediated signaling cascades that potentiate glucose-dependent insulin secretion from pancreatic beta cells.
In the central nervous system, incretin receptor activation in hypothalamic nuclei engages appetite-signaling circuitry, including POMC/CART neuron activation and NPY/AgRP neuron inhibition, as characterized in rodent and cell-based models. Peripheral effects include delayed gastric emptying through vagal afferent signaling and suppression of inappropriate glucagon secretion from pancreatic alpha cells. These descriptions summarize receptor-level pharmacology reported in the literature and are not statements of clinical efficacy or human benefit.
Key Research Findings
Published Study Highlights
- The alpha-aminoisobutyric acid substitution at position 8 is studied as a design strategy for resistance to dipeptidyl peptidase-4 cleavage
- Acylation at Lys26 with a C18 fatty diacid enables reversible, non-covalent albumin binding, extending circulating half-life in published pharmacokinetic models
- Characterized in receptor-binding studies as a selective agonist at a class B G-protein-coupled receptor with downstream cAMP/PKA signaling
- Biophysical work has examined the contribution of the fatty-acid linker to peptide self-association and albumin affinity
- Widely used as an analytical reference standard in LC-MS and HPLC method development for incretin-class peptides
Areas of Research Interest
Why Researchers Are Investigating This Compound
This compound has attracted significant research attention in the following areas. These represent active fields of scientific inquiry, not validated therapeutic claims. No medical benefits are stated or implied.
- Receptor pharmacology: used as a reference agonist in laboratory studies of class B GPCR binding kinetics and cAMP signal transduction
- Peptide stability research: the Aib substitution and albumin-binding linker are studied as protease-resistance and half-life-extension strategies
- Analytical method development: employed as a characterized reference standard for LC-MS/MS and HPLC assay validation
- Structural biology: investigated in studies of incretin receptor conformational states and ligand-receptor interfaces
Research Use Only
The information presented on this page is compiled from peer-reviewed scientific literature and is provided solely for educational and research purposes. This compound is intended exclusively for laboratory and scientific research use. It is not a drug, pharmaceutical, or dietary supplement. It is not intended to diagnose, treat, cure, or prevent any disease or medical condition. No claims of therapeutic efficacy are made or implied.
Researchers are advised to consult the original published studies referenced above for complete methodological details, study limitations, and the authors' own conclusions. Atlas Peptide Research does not endorse any specific research application and provides this information as a reference resource only.
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