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, a naturally occurring peptide originally isolated from amphibian skin secretions, is recognized for its unique structural and functional properties that have captured the interest of the scientific community. As a member of the bombesin-like peptide family, Heliodermin exhibits a distinct amino acid sequence that enables it to interact with specific receptors and influence various biological pathways. Its stability and bioactivity make it a valuable tool for researchers exploring peptide-mediated signaling, receptor pharmacology, and the modulation of physiological processes. The ability of Heliodermin to mimic or antagonize endogenous regulatory molecules further enhances its utility in experimental settings, particularly in the investigation of neuropeptide functions and intercellular communication.
Neuroscience research: Heliodermin serves as a powerful probe in neuroscience studies, especially those focused on the characterization of G protein-coupled receptors (GPCRs) and their associated signaling mechanisms. By binding to bombesin-like receptors, it facilitates the elucidation of receptor distribution, ligand specificity, and downstream signaling events in neuronal tissues. Researchers utilize this peptide to dissect the roles of neuropeptides in neurotransmitter release, synaptic plasticity, and neuroendocrine regulation. Its application extends to mapping receptor subtypes in the central and peripheral nervous systems, providing insights into the molecular basis of neural communication and the functional organization of neural circuits.
Signal transduction studies: The unique sequence and receptor affinity of Heliodermin make it a valuable tool for investigating intracellular signaling cascades. Scientists employ this peptide to activate or inhibit specific receptor-mediated pathways, thereby unraveling the complex web of cellular responses to extracellular stimuli. Through in vitro and ex vivo experiments, Heliodermin enables the detailed analysis of second messenger systems, protein kinase activation, and gene expression changes induced by peptide-receptor interactions. These studies contribute to a deeper understanding of how cells process information and adapt to environmental cues, supporting research into cellular physiology and pathophysiology.
Peptide-receptor interaction assays: In the field of pharmacology, Heliodermin is frequently used to assess the binding characteristics and functional responses of bombesin-like receptors. Radioligand binding assays, fluorescence-based techniques, and competition experiments leverage the specificity of this peptide to quantify receptor affinity, density, and selectivity. Such applications are instrumental in the screening of novel receptor modulators, the validation of ligand-receptor models, and the exploration of structure-activity relationships. By providing a reliable reference compound, Heliodermin supports the development of new tools for receptor characterization and drug discovery research.
Comparative physiology: Heliodermin is instrumental in comparative studies aimed at understanding the evolutionary conservation and divergence of peptide signaling systems across species. Its structural similarity to endogenous peptides in various vertebrates allows researchers to investigate functional homologies, receptor evolution, and the adaptation of neuropeptide systems. Experimental models ranging from amphibians to mammals benefit from the use of Heliodermin in cross-species analyses, which shed light on the fundamental principles governing peptide-mediated regulation of physiological processes such as metabolism, thermoregulation, and stress responses.
Endocrine research: The application of Heliodermin extends to the study of hormone secretion and regulation within the endocrine system. By modulating the activity of bombesin-like receptors in endocrine tissues, it enables researchers to probe the mechanisms underlying the release and synthesis of hormones such as gastrin, insulin, and growth hormone. These investigations provide valuable data on the interplay between neuropeptides and hormonal control, with implications for understanding energy homeostasis, appetite regulation, and metabolic adaptation. The versatility and specificity of Heliodermin continue to drive its adoption in diverse research fields, making it an indispensable tool for advancing our knowledge of peptide biology and intercellular communication.
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