[Ala5, β-Ala8]-Neurokinin A (4-10) CAS NO.127633-71-0

[Ala⁵, β‑Ala⁸]‑Neurokinin A (4‑10) is a synthetic, modified fragment of Neurokinin A designed for structure-activity relationship (SAR) studies in tachykinin receptor research. This analog features an alanine substitution at position 5 to simplify side-chain structure and a β-alanine at position 8 to increase backbone flexibility, both aimed at modulating receptor interaction and metabolic stability. Supplied as a lyophilized powder with ≥95% HPLC purity and low endotoxin levels, it serves as a tool compound for investigating NK receptor pharmacology, peptide design optimization, and the role of backbone flexibility in ligand-receptor engagement.

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TECHNICAL SPECIFICATIONS

Item	Specification
Product Name	[Ala5, β-Ala8]-Neurokinin A (4-10)
CAS NO.	127633-71-0
Appearance	White to off-white lyophilized powder
Molecular Formula	C35H56N8O9S
Molecular Weight	765g/mol
Purity (RP-HPLC)	≥ 95.0%
Solubility	Soluble in water, phosphate‑buffered saline (PBS), or dilute acetic acid (e.g., 0.1 % v/v). For best results, first dissolve in a small volume of 0.1 % acetic acid or sterile water to prepare a 0.1–1.0 mg/mL stock solution, then dilute with the desired assay buffer.
Endotoxin	< 1.0 EU/mg
Biological Activity	This analog is a modified fragment of Neurokinin A designed for structure-activity relationship (SAR) studies of tachykinin peptides. The Ala⁵ substitution may simplify the side-chain structure, while the β‑Ala⁸ introduction increases backbone flexibility, potentially altering receptor binding affinity, selectivity (primarily at NK₂ receptors), and metabolic stability compared to the native NKA(4‑10) sequence. Activity should be validated in relevant NK receptor binding or functional assays (e.g., calcium mobilization).
Storage Conditions	Lyophilized powder: Store desiccated at –20 °C or below, protected from light, for long‑term stability. Reconstituted solution: Aliquot and store at ≤ –20 °C; avoid repeated freeze‑thaw cycles.
Stock Location	Stock in USA
MOQ	1g

1.MECHANISM OF ACTION

The peptide acts as a tachykinin receptor ligand with potentially altered binding and signaling properties compared to native Neurokinin A. The Ala⁵ substitution reduces side-chain bulk, which may impact hydrophobic interactions with neurokinin receptors (primarily NK₂R), while the β‑Ala⁸ modification introduces increased conformational flexibility, potentially affecting receptor engagement, selectivity, and resistance to proteolytic degradation. Upon binding, it is expected to activate Gq/11-coupled pathways, leading to phospholipase C activation, IP₃ production, and calcium mobilization, though its specific agonist/antagonist profile and receptor selectivity must be empirically determined in functional assays.

2.PRODUCT INDICATIONS

This modified Neurokinin A fragment is indicated exclusively for research use in preclinical studies of tachykinin receptor pharmacology and peptide design. It is employed in structure-activity relationship studies to evaluate the effects of side-chain simplification and backbone flexibility on receptor binding affinity, selectivity, and metabolic stability. The product serves as a tool compound for screening NK receptor ligands, optimizing peptide therapeutics with improved pharmacokinetic properties, and investigating the pharmacophore requirements of tachykinin signaling. It is not intended for diagnostic, therapeutic, or clinical applications in humans or animals.

3.CLINICAL EFFICACY OF PRODUCT

As a research reagent for SAR studies, [Ala⁵, β‑Ala⁸]‑Neurokinin A (4‑10) has no established clinical efficacy for therapeutic use in human patients. The product has not undergone clinical development, regulatory approval, or safety evaluation for any medical indication. While it contributes to the understanding of tachykinin receptor pharmacology and peptide design principles, particularly regarding the impact of backbone flexibility on ligand properties, it remains an investigational tool for basic research. Its utility is confined to laboratory applications, with no proven clinical benefits or safety profile in humans.

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