Heliodermin is a frog-derived peptide belonging to the vasoactive intestinal peptide family, characterized by high helix-forming propensity and multiple charged residues. Its sequence supports binding to class B GPCR models in vitro. Researchers analyze conformational ensembles, receptor-contact residues, and proteolytic stability. Applications include neuropeptide-motif research, receptor-ligand mapping, and structural characterization.
CAT No: PI-019
CAS No:89468-62-2
Synonyms/Alias:Helodermin;Exendin 2;Heliodermin;89468-62-2;DTXSID00237753;Helospectin I, 5-L-isoleucine-8-L-glutamine-9-L-glutamine-24-L-alanine-30-L-arginine-34-de-L-arginine-36-L-prolinamide-37-de-L-serine-38-de-L-serine-;H1V1OM98DI;GTPL2280;BDBM82394;DTXCID50160244;NCGC00167249-01;CAS_89468-62-2;HIS-SER-ASP-ALA-ILE-PHE-THR-GLU-GLU-TYR-SER-LYS-LEU-LEU-ALA-LYS-LEU-ALA-LEU-GLN-LYS-TYR-LEU-ALA-SER-ILE-LEU-GLY-SER-ARG-THR-SER-PRO-PRO-PRONH2;
Heliodermin is a synthetic peptide originally isolated from the skin secretions of the European yellow-bellied toad, Bombina variegata. As a member of the bombesin-like peptide family, it exhibits distinctive structural motifs and bioactivity relevant to neuropeptide research. Its unique amino acid sequence and affinity for certain G protein-coupled receptors have made it a valuable molecular tool in the study of peptide-receptor interactions, signal transduction pathways, and neuropharmacology. The compound's stability and defined structure support its use in a variety of in vitro and in vivo experimental designs, making it a significant asset in the field of peptide science.
Receptor binding studies: Heliodermin serves as a potent ligand for bombesin receptor subtypes, particularly those expressed in neuronal and peripheral tissues. Researchers utilize it to probe the pharmacological properties, binding affinities, and activation mechanisms of these receptors. By enabling precise mapping of ligand-receptor interactions, the peptide supports the elucidation of signaling cascades and functional outcomes associated with bombesin-like peptides, contributing to a deeper understanding of neuropeptide-mediated communication.
Signal transduction research: The peptide is frequently employed to investigate intracellular signaling pathways activated by bombesin receptor engagement. Experimental applications include analysis of second messenger systems such as phospholipase C activation, calcium mobilization, and downstream phosphorylation events. Its defined structure and receptor selectivity allow for controlled studies of G protein-coupled receptor (GPCR) signaling dynamics, offering insights into cellular responses that are relevant to both basic neuroscience and pharmacological modulation.
Peptide structure-activity relationship (SAR) analysis: Heliodermin provides a robust model for SAR studies, where systematic modifications to its amino acid sequence can reveal critical determinants of receptor binding and functional selectivity. By comparing the biological activity of native and analog forms, researchers can identify key residues responsible for potency and specificity. These investigations inform the rational design of novel peptide ligands with tailored pharmacological profiles, advancing both fundamental peptide chemistry and the development of research tools.
Neuropeptide functional assays: In neurobiology and endocrinology research, the peptide is used as a reference agonist in a variety of functional assays, including studies of neurotransmitter release, hormone secretion, and neuronal excitability. Its ability to mimic endogenous bombesin-like peptides allows for the assessment of physiological responses in cultured cells, tissue preparations, and animal models. This facilitates the dissection of neuropeptide roles in regulatory circuits and homeostatic mechanisms.
Peptide synthesis validation: Heliodermin is also valuable in the context of synthetic peptide production and quality control. Its well-characterized sequence and bioactivity make it a suitable standard for validating peptide synthesis protocols, purification methods, and analytical techniques such as mass spectrometry and high-performance liquid chromatography. By serving as a benchmark compound, it aids laboratories in ensuring the reliability and reproducibility of peptide-based experiments, which is critical for advancing research in peptide science.
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