[bAla8]-Neurokinin A(4-10) is a neurokinin 2 (NK2) receptor agonist.
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CAT No: R1117
CAS No:122063-01-8
Synonyms/Alias:[bAla8]-Neurokinin A(4-10);122063-01-8;MEN 10210;L-Methioninamide, L-alpha-aspartyl-L-seryl-L-phenylalanyl-L-valyl-beta-alanyl-L-leucyl-;(3S)-3-amino-4-[[(2S)-1-[[(2S)-1-[[(2S)-1-[[3-[[(2S)-1-[[(2S)-1-amino-4-methylsulfanyl-1-oxobutan-2-yl]amino]-4-methyl-1-oxopentan-2-yl]amino]-3-oxopropyl]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;(3S)-3-AMINO-3-{[(1S)-1-{[(1S)-1-{[(1S)-1-[(2-{[(1S)-1-{[(1S)-1-CARBAMOYL-3-(METHYLSULFANYL)PROPYL]CARBAMOYL}-3-METHYLBUTYL]CARBAMOYL}ETHYL)CARBAMOYL]-2-METHYLPROPYL]CARBAMOYL}-2-PHENYLETHYL]CARBAMOYL}-2-HYDROXYETHYL]CARBAMOYL}PROPANOIC ACID;MFCD00143686;Asp-Ser-Phe-Val-beta-Ala-Leu-Met-NH2;CHEMBL1875296;HY-P1031;(b-Ala8)-Neurokinin A (4-10);AKOS024456720;CS-7598;NCGC00167336-01;AS-80269;DA-59741;L-Methioninamide,l-a-aspartyl-L-seryl-L-phenylalanyl-L-valyl-b-alanyl-L-leucyl-;(5S,8S,15S,18S,21S,24S)-24-amino-18-benzyl-5-carbamoyl-21-(hydroxymethyl)-8-isobutyl-15-isopropyl-7,10,14,17,20,23-hexaoxo-2-thia-6,9,13,16,19,22-hexaazahexacosan-26-oic acid;
[bAla8]-Neurokinin A(4-10) is a synthetic peptide analog derived from the C-terminal fragment of Neurokinin A, a member of the tachykinin neuropeptide family. Incorporating a beta-alanine (bAla) substitution at the eighth position, this modified sequence offers unique structural and functional attributes that distinguish it from the native peptide. The alteration is designed to influence receptor binding dynamics, metabolic stability, and conformational properties, making the analog a valuable tool for probing neuropeptide signaling pathways. Researchers leverage such peptide derivatives to dissect the complex roles of tachykinins in neurobiology, receptor pharmacology, and peptide structure-activity relationships.
Peptide receptor pharmacology: The [bAla8]-Neurokinin A(4-10) analog is widely utilized in studies investigating the pharmacological properties of tachykinin receptors, particularly the neurokinin 2 (NK2) subtype. By introducing a non-natural amino acid at a key position, the peptide enables researchers to assess the impact of structural modifications on receptor selectivity, binding affinity, and signal transduction. These studies provide critical insights into the molecular determinants of peptide-receptor interactions, facilitating the development of more selective ligands and advancing our understanding of neuropeptide-mediated signaling mechanisms.
Structure-activity relationship analysis: The presence of beta-alanine in the peptide backbone makes this analog an important probe for elucidating structure-activity relationships within the tachykinin family. Systematic comparison of the biological activities of native and modified peptides allows researchers to map functional domains, identify crucial residues for receptor activation, and understand the role of peptide conformation in biological efficacy. Such analyses are essential for rational peptide design and for advancing the field of neuropeptide research.
Metabolic stability and degradation studies: The incorporation of a beta-alanine residue offers an opportunity to investigate how noncanonical amino acids influence peptide stability and enzymatic degradation. Researchers employ [bAla8]-Neurokinin A(4-10) in in vitro and ex vivo assays to evaluate resistance to peptidases and to characterize metabolic pathways relevant to tachykinin peptides. These studies inform strategies for enhancing peptide half-life and bioavailability in experimental systems, which is critical for applications in neuropharmacology and peptide-based tool development.
Neuropeptide signaling pathway elucidation: By serving as a selective ligand or functional probe, the modified peptide aids in dissecting the roles of tachykinin signaling in neuronal and non-neuronal tissues. Functional assays utilizing this analog can help delineate downstream signaling cascades, receptor subtype contributions, and cellular responses to neuropeptide stimulation. The ability to modulate or mimic endogenous peptide action with tailored analogs greatly expands experimental options for researchers exploring complex neurobiological processes.
Peptide synthesis and analog development: [bAla8]-Neurokinin A(4-10) is also valuable as a reference compound or intermediate in the synthesis of further peptide analogs. Its defined sequence and documented modifications serve as a template for designing novel derivatives with altered physicochemical or biological properties. Synthetic chemists and peptide engineers use such analogs to optimize peptide libraries, develop new research tools, and explore innovative modifications that enhance peptide performance in diverse biochemical applications.
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