Kassinin is a peptide derived from the skin of the African frog Kassina senegalensis. It belongs to tachykinin family of neuropeptides. It is secreted as a defense response, and is involved in neuropeptide signalling.
CAT No: 10-101-66
CAS No:63968-82-1
Synonyms/Alias:KASSININ;63968-82-1;DTXSID50895029;GTPL2088;SCHEMBL20639320;BDBM81943;DTXCID801324588;L-.ALPHA.-ASPARTYL-L-VALYL-L-PROLYL-L-LYSYL-L-SERYL-L-.ALPHA.-ASPARTYL-L-GLUTAMINYL-L-PHENYLALANYL-L-VALYLGLYCYL-L-LEUCYL-L-METHIONINAMIDE;L-METHIONINAMIDE, L-.ALPHA.-ASPARTYL-L-VALYL-L-PROLYL-L-LYSYL-L-SERYL-L-.ALPHA.-ASPARTYL-L-GLUTAMINYL-L-PHENYLALANYL-L-VALYLGLYCYL-L-LEUCYL-;L-Methioninamide, L-alpha-aspartyl-L-valyl-L-prolyl-L-lysyl-L-seryl-L-alpha-aspartyl-L-glutaminyl-L-phenylalanyl-L-valylglycyl-L-leucyl-;CAS_45749;NSC_45749;DA-64713;Q6374755;alpha-aspartylvalylprolyllysylseryl-alpha-aspartylglutaminylphenylalanylvalylglycylleucylmethioninamide;
Chemical Name:(3S)-3-amino-4-[[(2S)-1-[(2S)-2-[[(2S)-6-amino-1-[[(2S)-1-[[(2S)-1-[[(2S)-5-amino-1-[[(2S)-1-[[(2S)-1-[[2-[[(2S)-1-[[(2S)-1-amino-4-methylsulfanyl-1-oxobutan-2-yl]amino]-4-methyl-1-oxopentan-2-yl]amino]-2-oxoethyl]amino]-3-methyl-1-oxobutan-2-yl]amino]-1-oxo-3-phenylpropan-2-yl]amino]-1,5-dioxopentan-2-yl]amino]-3-carboxy-1-oxopropan-2-yl]amino]-3-hydroxy-1-oxopropan-2-yl]amino]-1-oxohexan-2-yl]carbamoyl]pyrrolidin-1-yl]-3-methyl-1-oxobutan-2-yl]amino]-4-oxobutanoic acid
Kassinin is a naturally occurring tachykinin peptide originally isolated from the skin of the African frog Kassina senegalensis. Recognized for its distinctive amino acid sequence and robust biological activity, Kassinin has become a valuable tool in neurobiological and physiological research. Its structural features, including a conserved C-terminal motif, enable it to interact selectively with specific neurokinin receptors, making it an important probe for studying peptide-receptor interactions. Researchers are drawn to Kassinin for its ability to induce measurable physiological responses in experimental models, providing insights into the mechanisms of neurotransmission and smooth muscle regulation. The peptide's stability and compatibility with a range of assay systems further enhance its utility in laboratory investigations, supporting a broad spectrum of scientific applications.
Neuropharmacology research: Kassinin is extensively utilized in neuropharmacology to elucidate the roles of tachykinin peptides in the central and peripheral nervous systems. By applying it to tissue preparations or in vivo models, scientists can investigate its effects on neuronal signaling pathways, synaptic transmission, and receptor specificity. The peptide's affinity for neurokinin receptors, particularly NK2 and NK3 subtypes, allows for detailed mapping of receptor distribution and function. These studies contribute to a greater understanding of how tachykinins modulate pain perception, emotional responses, and neurogenic inflammation, facilitating the development of new hypotheses regarding neurotransmitter systems.
Smooth muscle physiology: In the field of smooth muscle research, Kassinin is employed to characterize contractile responses in a variety of tissues, including gastrointestinal, respiratory, and vascular systems. Researchers utilize the peptide to induce and measure muscle contractions, thereby assessing the functional roles of tachykinin receptors in mediating smooth muscle tone. These experiments help delineate the signaling cascades that govern motility and secretion, offering valuable data for comparative studies across species. The use of Kassinin in isolated organ bath assays or tissue strip preparations enables precise quantification of its pharmacological effects, advancing knowledge of muscle physiology.
Signal transduction studies: As a potent activator of G protein-coupled receptors, Kassinin serves as a model ligand for dissecting intracellular signaling pathways. Experimental application of the peptide allows investigators to monitor downstream events such as phospholipase C activation, calcium mobilization, and second messenger production. By analyzing these cellular responses, researchers can unravel the mechanisms by which tachykinins influence cell function and communication. Insights gained from these studies inform broader research into peptide hormone signaling and receptor pharmacodynamics, supporting the design of targeted molecular probes and antagonists.
Comparative endocrinology: Kassinin provides a unique perspective in comparative endocrinology, where it is used to explore the evolutionary conservation and divergence of peptide signaling systems. Scientists compare its biological effects across different animal models, examining variations in receptor expression, tissue responsiveness, and physiological outcomes. These investigations shed light on the adaptive significance of tachykinin peptides in vertebrate evolution and help identify conserved motifs critical for receptor binding. The data generated contribute to the broader field of peptide hormone research, highlighting the diversity and complexity of neuropeptide function.
Peptide structure-activity relationship (SAR) analysis: The well-defined sequence and bioactivity of Kassinin make it an ideal candidate for SAR studies aimed at identifying key structural determinants of receptor binding and activation. By synthesizing and testing analogs with systematic modifications, researchers can pinpoint amino acid residues essential for biological function. These structure-activity investigations facilitate the rational design of novel peptide ligands with enhanced selectivity or potency, expanding the toolkit available for receptor characterization and drug discovery. The insights gained from SAR studies using Kassinin inform the broader understanding of peptide-receptor interactions and support the development of innovative research tools.
In summary, Kassinin stands as a versatile and impactful peptide in scientific research, supporting advancements in neuropharmacology, smooth muscle physiology, signal transduction, comparative endocrinology, and structure-activity relationship analysis. Its unique properties and biological relevance enable researchers to address fundamental questions in peptide signaling and receptor function, driving innovation across multiple disciplines in the life sciences.
Tachykinins are among the most widely-studied families of regulatory peptides characterized by a highly-conserved C-terminal -Phe-X-Gly-Leu-Met.amide motif, which also constitutes the essential bioactive core. The amphibian skin has proved to be a rich source of these peptides with physalaemin from the skin of Physalaemus fuscomaculatus representing the archetypal aromatic tachykinin (X=Tyr or Phe) and kassinin from the skin of Kassina senegalensis representing the archetypal aliphatic tachykinin in which X=Val or Ile. Despite the primary structures of both mature peptides having been known for at least 30 years, neither the structures nor organizations of their biosynthetic precursors have been reported. Here we report the structure and organization of the biosynthetic precursor of kassinin deduced from cDNA cloned from a skin secretion library. In addition, a second precursor cDNA encoding the novel kassinin analog (Thr(2), Ile(9))-kassinin was identified as was the predicted mature peptide in skin secretion. Both transcripts exhibited a high degree of nucleotide sequence similarity and of open-reading frame translated amino acid sequences of putative precursor proteins. The translated preprotachykinins each consisted of 80 amino acid residues encoding single copies of either kassinin or its site-substituted analog. Synthetic replicates of each kassinin were found to be active on rat urinary bladder smooth muscle at nanomolar concentrations. The structural organization of both preprotachykinins differs from that previously reported for those of Odorrana grahami skin indicating a spectrum of diversity akin to that established for amphibian skin preprobradykinins.
Wang, L., Zhou, M., Lynch, L., Chen, T., Walker, B., & Shaw, C. (2009). Kassina senegalensis skin tachykinins: Molecular cloning of kassinin and (Thr 2, Ile 9)-kassinin biosynthetic precursor cDNAs and comparative bioactivity of mature tachykinins on the smooth muscle of rat urinary bladder. Biochimie, 91(5), 613-619.
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