Kassinin - CAS 63968-82-1
Category: Inhibitor
Not Intended for Therapeutic Use. For research use only.
Molecular Formula:
Molecular Weight:
Neurokinin Receptor
Kassinin, a tachykinin peptide derived from the Kassina frog, is secreted as a defense response, and is involved in neuropeptide signalling and shows selectivity for NK2 over NK1 in mammals.
3-amino-4-[[1-[2-[[6-amino-1-[[1-[[1-[[5-amino-1-[[1-[[1-[[2-[[1-[(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]ami; KASSININ; CID45749; LS-187057; LS-187667; 63968-82-1; 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-; H-Asp-Val-Pro-Lys-Ser-Asp-Gln-Phe-Val-Gly-Leu-Met-NH2
Store in a cool and dry place (or refer to the Certificate of Analysis).
Boiling Point:
1730.2±65.0 ℃ at 760 Torr
1.305±0.06 g/cm3
Canonical SMILES:
1.A comparison of the effects of three substance P antagonists on tachykinin-stimulated [3H]-acetylcholine release in the guinea-pig ileum.
Featherstone RL;Fosbraey P;Morton IK Br J Pharmacol. 1986 Jan;87(1):73-7.
The potencies of three tachykinin antagonists [D-Pro4,D-Trp7,9,10]SP(4-11), [D-Arg1,D-Pro2,D-Trp7,9,Leu11]SP(1-11) and [D-Arg1,D-Trp7,9,Leu11]SP(1-11) (spantide) against eledoisin were examined in the guinea-pig ileum myenteric plexus, where a continuous superfusion system was employed to examine evoked release of [3H]-acetylcholine [( 3H]-ACh]); effects on mechanical activity of the preparations were also measured. Eledoisin was chosen as the standard tachykinin agonist since the rank order of potency observed in evoking release was eledoisin, kassinin, substance P, physalaemin; on this basis is may be presumed that an 'SP-E' type receptor was involved in the release process. The two undecapeptide antagonists both significantly reduced the response to eledoisin (10 nM) as assessed by both [3H]-ACh release and mechanical activity which under these conditions was largely dependent on ACh release, and the response levels could be restored by increasing the concentration of eledoisin to 100 nM. The pA2 values for the two antagonists were estimated as 5.3 for [D-Arg1,D-Pro2,D-Trp7,9,Leu11]SP(1-11) and 5.2 for [D-Arg1,D-Trp7,9,Leu11]SP(1-11). [D-Pro4,D-Trp7,9,10]SP(4-11) was markedly less potent with a pA2 value of less than 4.
2.The rat isolated portal vein: a preparation sensitive to neurokinins, particularly neurokinin B.
Mastrangelo D;Mathison R;Huggel HJ;Dion S;D'Orléans-Juste P;Rhaleb NE;Drapeau G;Rovero P;Regoli D Eur J Pharmacol. 1987 Feb 24;134(3):321-6.
The rat isolated portal vein is a pharmacological preparation more sensitive to neurokinin B than to any other neurokinin or tachykinin. The preparation is more sensitive to C-terminal partial sequences of substance P (SP) particularly SP-(6-11) than to the whole undecapeptide. The order of potency of neurokinins is as follows: neurokinin B greater than neurokinin A greater than substance P. The preparation shows high sensitivity also to kassinin and eledoisin. Comparative tests performed with strips of the rat portal vein suspended in a microbath under continuous perfusion (system 1) or in ordinary baths for isolated smooth muscles (system 2) have given similar results and have shown that the myotropic effect of neurokinin B is not modified by a variety of antagonists of endogenous agents as well as by inhibitors of the arachidonic acid cascade. The present results suggest that neurokinin B contracts the rat portal vein by activating specific receptors, presumably located on the smooth muscle membrane, different from those of biologically active amines and peptides which are active stimulants of the vein. Neurokinin B is ten times more active than neurokinin A and at least 100 times more than substance P.
3.Pharmacological and biochemical investigation of receptors for the toad gut tachykinin peptide, bufokinin, in its species of origin.
Liu L;Warner FJ;Conlon JM;Burcher E Naunyn Schmiedebergs Arch Pharmacol. 1999 Aug;360(2):187-95.
This is the first report of the development of a new radioligand [125I]Bolton-Hunter bufokinin ([125I]BH-bufokinin) and its use in the characterisation of tachykinin receptors in the small intestine of the cane toad, Bufo matrinus. The binding of [125I]BH-bufokinin to toad intestinal membranes was rapid, saturable, of high affinity and to a single population of binding sites with KD 0.57 nM and Bmax 3.1 fmol mg wet weight tissue(-1). The rank order of affinity of tachykinins to compete for [125I]-BH bufokinin binding revealed similarities with that of the mammalian NK1 receptor, being bufokinin (IC50, 1.7 nM)>physalaemin (6.7 nM)>substance P (SP, 10.7 nM)> or =neuropeptide gamma (NPgamma, 12.4 nM)> or =kassinin (17.8 nM)>scyliorhinin I (35.3 nM)> or =eledoisin (40.6 nM)> or =carassin (43.2 nM)> or =neurokinin A (NKA, 57.8 nM)> or =neurokinin B (NKB, 77.5 nM)>scyliorhinin II (338 nM). The mammalian NK3-selective agonist senktide was a very weak competitor. The radioligand [125I]neurokinin A showed no specific binding to toad intestinal membranes. In the toad isolated small intestine, the maximum contractile response to bufokinin was over 150% greater than that to acetylcholine in longitudinal muscle, whereas responses to bufokinin and acetylcholine were similar in circular muscle.
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CAS 63968-82-1 Kassinin

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