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 peptide belonging to the tachykinin family, originally isolated from amphibian sources. As a neuropeptide, it is composed of a specific sequence of amino acids that confer unique biological properties, particularly in relation to neurotransmission and smooth muscle modulation. Its structural characteristics and sequence homology with other tachykinins, such as substance P and neurokinin A, have made it a valuable tool in neurobiological and pharmacological research. The ability of kassinin to interact with neurokinin receptors and modulate physiological responses has established its significance in studies exploring peptide-receptor interactions, signal transduction, and the broader field of peptide-mediated cellular communication.
Neuroscience research: Kassinin is widely utilized in neuroscience investigations aimed at elucidating the functional dynamics of tachykinin receptors within the central and peripheral nervous systems. By serving as a selective ligand for neurokinin receptors, particularly NK2 subtypes, it enables researchers to dissect the molecular mechanisms underlying neurotransmitter release, synaptic plasticity, and neuronal excitability. Its application in electrophysiological assays and receptor binding studies provides critical insights into the modulation of neural circuits and the role of tachykinins in sensory processing, pain perception, and neurogenic inflammation.
Pharmacological profiling: In pharmacological studies, kassinin functions as a reference compound for characterizing the specificity, affinity, and efficacy of neurokinin receptor agonists and antagonists. Its well-defined activity profile facilitates the comparative assessment of novel drug candidates targeting tachykinin pathways. By employing this peptide in in vitro assays, researchers can quantify receptor activation, analyze downstream signaling cascades, and evaluate the pharmacodynamic properties of experimental compounds, thereby advancing the development of therapeutic agents that modulate neuropeptide signaling.
Smooth muscle physiology: The peptide is frequently applied in research focused on smooth muscle contractility and gastrointestinal motility. Its potent agonistic action on neurokinin receptors expressed in smooth muscle tissues allows for the investigation of contraction mechanisms, receptor subtype distribution, and the physiological regulation of visceral function. Experimental models employing kassinin help clarify the contributions of tachykinins to gut motility, airway responsiveness, and vascular tone, supporting a deeper understanding of peptide-mediated control of smooth muscle systems.
Peptide-receptor interaction studies: Kassinin serves as an essential probe in structural and functional analyses of peptide-receptor interactions. Its defined sequence and receptor selectivity make it suitable for mapping ligand binding domains, elucidating receptor conformational changes, and exploring the determinants of peptide specificity. Techniques such as site-directed mutagenesis, molecular modeling, and biophysical assays benefit from the use of this peptide to reveal the structural basis of tachykinin recognition and signal initiation at the molecular level.
Peptide synthesis and analog development: The unique sequence and biological activity of kassinin have inspired the synthesis of analogs and modified peptides for structure-activity relationship (SAR) studies. Researchers utilize it as a template to design derivatives with altered receptor selectivity, stability, or functional properties. Such efforts contribute to the optimization of peptide-based probes and the identification of novel ligands with tailored pharmacological profiles, enhancing the toolkit available for research in neurobiology, pharmacology, and peptide chemistry.
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.
4. Autoinhibition and phosphorylation-induced activation of phospholipase C-γ isozymes
5. Immune-awakening Saccharomyces-inspired nanocarrier for oral target delivery to lymph and tumors
If you have any peptide synthesis requirement in mind, please do not hesitate to contact us at . We will endeavor to provide highly satisfying products and services.
Creative Peptides is a trusted CDMO partner specializing in high-quality peptide synthesis, conjugation, and manufacturing under strict cGMP compliance. With advanced technology platforms and a team of experienced scientists, we deliver tailored peptide solutions to support drug discovery, clinical development, and cosmetic innovation worldwide.
From custom peptide synthesis to complex peptide-drug conjugates, we provide flexible, end-to-end services designed to accelerate timelines and ensure regulatory excellence. Our commitment to quality, reliability, and innovation has made us a preferred partner across the pharmaceutical, biotechnology, and personal care industries.
Read More