Neurokinin A(4-10) is a truncated tachykinin fragment containing key residues that influence receptor-binding motifs. The shortened peptide supports examination of charge distribution, aromatic packing, and backbone dynamics. Researchers apply it to map core sequence contributions to neuropeptide signaling. Its compact structure improves resolution in structural analyses.
CAT No: R1532
CAS No:97559-35-8
Synonyms/Alias:neurokinin A(4-10);97559-35-8;Nka-(4-10);CHEMBL126294;(3S)-3-amino-4-[[(2S)-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]-3-hydroxy-1-oxopropan-2-yl]amino]-4-oxobutanoic acid;L-Methioninamide, L-alpha-aspartyl-L-seryl-L-phenylalanyl-L-valylglycyl-L-leucyl-;DTXSID50913838;HY-P0236;Asp-Ser-Phe-Val-Gly-Leu-Met-NH2;BDBM50001451;(5S,8S,14S,17S,20S,23S)-23-amino-17-benzyl-5-carbamoyl-20-(hydroxymethyl)-8-isobutyl-14-isopropyl-7,10,13,16,19,22-hexaoxo-2-thia-6,9,12,15,18,21-hexaazapentacosan-25-oic acid;23-Amino-17-benzyl-7,10,13,16,19,22-hexahydroxy-5-[hydroxy(imino)methyl]-20-(hydroxymethyl)-8-(2-methylpropyl)-14-(propan-2-yl)-2-thia-6,9,12,15,18,21-hexaazapentacosa-6,9,12,15,18,21-hexaen-25-oic acid;3-Amino-N-(1-{1-[1-({[1-(1-carbamoyl-3-methylsulfanyl-propylcarbamoyl)-3-methyl-butylcarbamoyl]-methyl}-carbamoyl)-2-methyl-propylcarbamoyl]-2-phenyl-ethylcarbamoyl}-2-hydroxy-ethyl)-succinamic acid;
Neurokinin A(4-10) is a synthetic peptide fragment derived from the C-terminal region of the neuropeptide Neurokinin A, a member of the tachykinin family. Characterized by its specific amino acid sequence, this peptide is notable for its ability to interact selectively with neurokinin receptors, particularly the NK2 subtype. Its truncated structure retains significant biological activity, making it a valuable molecular tool in neurobiology and pharmacology research. The fragment is frequently employed to probe the physiological roles of tachykinins in the central and peripheral nervous systems, as well as to dissect the structure-activity relationships governing receptor-ligand interactions within this peptide family.
Receptor binding studies: As a well-defined peptide ligand, Neurokinin A(4-10) is extensively utilized in receptor binding assays to characterize the affinity and selectivity of neurokinin receptors, especially NK2. Researchers use this fragment to map binding domains, evaluate competitive inhibition, and distinguish between receptor subtypes in both in vitro and ex vivo preparations. Its defined sequence allows for precise interrogation of the molecular determinants underlying tachykinin-receptor interactions, facilitating the development of more selective receptor modulators.
Signal transduction research: The peptide serves as an effective stimulus in studies investigating intracellular signaling cascades triggered by neurokinin receptor activation. By applying Neurokinin A(4-10) to cultured neuronal or smooth muscle cells, investigators can monitor downstream events such as calcium mobilization, phospholipase C activation, or MAP kinase pathway engagement. These experiments elucidate the mechanisms by which tachykinins regulate cellular responses, contributing to a deeper understanding of neuropeptide signal transduction.
Functional assays in smooth muscle physiology: Due to its retained bioactivity, Neurokinin A(4-10) is frequently applied in functional assays examining contractile responses in isolated smooth muscle tissues. Researchers employ the peptide to evaluate the pharmacological properties of NK2 receptor-mediated contraction, assess desensitization phenomena, and compare the efficacy of novel antagonists. Such studies are instrumental in clarifying the physiological roles of tachykinins in gastrointestinal, respiratory, and genitourinary systems.
Neuropeptide metabolism investigations: The defined structure of Neurokinin A(4-10) makes it a suitable substrate for studies on peptide degradation and metabolic stability. Enzymatic assays using this fragment help identify peptidases responsible for tachykinin catabolism, determine cleavage sites, and assess the impact of structural modifications on metabolic half-life. These insights are valuable for designing peptide analogs with improved stability for research applications.
Structure-activity relationship (SAR) analysis: The C-terminal fragment is an important tool in SAR studies aimed at dissecting the functional domains of tachykinin peptides. By comparing the biological activities of Neurokinin A(4-10) with those of full-length Neurokinin A and other truncated analogs, researchers gain insights into the minimal sequence requirements for receptor activation and selectivity. These findings inform the rational design of peptide-based ligands with tailored pharmacological profiles for use in neuropharmacological research.
1. Cell-based adhesion assays for isolation of snake venom’s integrin antagonists
5. Urinary Metabolites Associated with Blood Pressure on a Low-or High-Sodium Die
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