Bombesin is a tetradecapeptide originally isolated from frog skin; plays an important role in the release of gastrin and the activation of G-protein receptors.
CAT No: R1243
CAS No:31362-50-2
Synonyms/Alias:31362-50-2;Bombesin 14;PX9AZU7QPK;UNII-PX9AZU7QPK;BOMBESIN [MI];Alytesin, 2-L-glutamine-6-L-asparagine-;CCRIS 3334;pGlu-Gln-Arg-Leu-Gly-Asn-Gln-Trp-Ala-Val-Gly-His-Leu-Met-NH2;5-OXO-PRO-GLN-ARG-LEU-GLY-ASN-GLN-TRP-ALA-VAL-GLY-HIS-LEU-MET-NH2;L-METHIONINAMIDE, 5-OXO-L-PROLYL-L-GLUTAMINYL-L-ARGINYL-L-LEUCYLGLYCYL-L-ASPARAGINYL-L-GLUTAMINYL-L-TRYPTOPHYL-L-ALANYL-L-VALYLGLYCYL-L-HISTIDYL-L-LEUCYL-;Bombesin trifluoroacetate salt;bombesin-acetate;MFCD00167514;CHEMBL437027;DTXSID1037149;H-{PyroE}QRLGNQWAVGHLM-NH2;5-oxoPro-Gln-Arg-Leu-Gly-Asn-Gln-Trp-Ala-Val-Gly-His-Leu-MetNH2;AKOS037645006;AS-56033;DA-51337;FB108614;Bombesin acetate salt hydrate, >=97% (HPLC);D81821;H- pGlu-Gln-Arg-Leu-Gly-Asn-Gln-Trp-Ala-Val-Gly-His-Leu-Met-NH2;Pyr-Gln-Arg-Leu-Gly-Asn-Gln-Trp-Ala-Val-Gly-His-Leu-Met-NH2; pE-QRLGNQWAVGHLM-NH2;(S)-N1-((5S,8S,11S,17S,20S,23S,26S,29S,35S,38S)-11-((1H-Imidazol-5-yl)methyl)-23-((1H-indol-3-yl)methyl)-43-amino-29-(2-amino-2-oxoethyl)-26-(3-amino-3-oxopropyl)-5-carbamoyl-43-imino-8,35-diisobutyl-17-isopropyl-20-methyl-7,10,13,16,19,22,25,28,31,34,37-;
Bombesin is a biologically active peptide originally isolated from the skin of amphibians, recognized for its potent ability to bind and activate specific G protein-coupled receptors in mammalian tissues. Structurally characterized by a unique amino acid sequence, bombesin exhibits significant homology to mammalian peptides such as gastrin-releasing peptide (GRP) and neuromedin B, which are involved in diverse physiological processes. Its role as a signaling molecule has made it a valuable tool in the study of neuroendocrine regulation, gastrointestinal physiology, and peptide-receptor interactions. Researchers utilize bombesin to probe fundamental mechanisms of cell signaling, growth factor regulation, and neuropeptide function, making it a critical reagent in both basic and applied biochemical research.
Receptor Characterization: Bombesin is widely employed in studies aimed at characterizing peptide receptor subtypes, particularly the bombesin receptor family, which includes BB1, BB2 (GRP receptor), and BB3. By serving as a high-affinity ligand, it enables detailed analysis of receptor binding kinetics, specificity, and downstream signaling events in various tissues and cell lines. Such research is essential for elucidating the molecular underpinnings of receptor-mediated signal transduction and for mapping receptor distribution in normal and pathological states.
Cell Signaling Research: The peptide is instrumental in investigations of intracellular signaling cascades initiated by neuropeptides. Upon binding to its receptors, bombesin triggers a cascade of events involving phospholipase C activation, increased intracellular calcium, and protein kinase C modulation. These pathways are studied to uncover how peptide hormones regulate cellular proliferation, differentiation, and gene expression. Its use in cell-based assays has provided insights into the mechanisms of mitogenic stimulation and neuroendocrine communication.
Gastrointestinal Physiology Studies: As a potent stimulator of gastrointestinal motility and secretion, bombesin is used to model and dissect the regulatory roles of neuropeptides in digestive system function. Researchers apply it to in vitro and ex vivo preparations to assess its effects on smooth muscle contraction, enzyme release, and hormone secretion. These studies contribute to a deeper understanding of gut-brain axis signaling and the neurochemical control of digestive physiology.
Peptide Structure-Activity Relationship (SAR) Analysis: The unique sequence and bioactivity of bombesin make it a prime candidate for SAR studies in peptide chemistry. Synthetic analogs and modified derivatives are evaluated to determine the structural elements critical for receptor binding and activation. Such research supports the rational design of novel ligands with tailored affinity and selectivity profiles, advancing both fundamental peptide science and the development of specialized research tools.
Radioligand Binding and Imaging Applications: Labeled derivatives of bombesin, including radioisotope-conjugated forms, are utilized in radioligand binding assays and imaging studies. These applications enable the quantitative measurement of receptor density, affinity, and distribution in tissues and experimental models. The use of radiolabeled peptides has also facilitated the development of advanced techniques for visualizing neuropeptide receptor dynamics and exploring receptor-mediated processes in situ.
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