$90.00 - $90.00
MEN 10207, also known as [Tyr5,D-Trp6,8,9,Arg10]-Neurokinin A (4-10), is a seven-residue synthetic tachykinin analog developed as a selective peptide antagonist of the NK2 receptor.
Its sequence, Asp-Tyr-D-Trp-Val-D-Trp-D-Trp-Arg-NH₂, differs extensively from native NKA (4-10) and contains three D-tryptophan residues that are central to its antagonist pharmacology.
Product Information
| Property | Specification |
|---|---|
| Product Name | [Tyr5,D-Trp6,8,9,Arg10]-Neurokinin A (4-10) |
| Catalog No. | AS2574 |
| Common Name | MEN 10207 |
| CAS No. | 126050-12-2 |
| Sequence | Asp-Tyr-D-Trp-Val-D-Trp-D-Trp-Arg-NH₂ |
| One-Letter Representation | DYwVwwR-NH₂ |
| Peptide Length | 7 residues |
| Molecular Formula | C57H68N14O10 |
| Molecular Weight | Approximately 1109.3 Da |
| Pharmacological Role | NK2 receptor antagonist |
Three D-Trp Residues Drive the Antagonist Scaffold
MEN 10207 replaces several residues from native NKA(4-10) with bulky aromatic D-tryptophans. Structure–activity studies showed that the simultaneous presence of all three D-Trp residues is important for both receptor affinity and NK2 selectivity.
NK2-Selective Tachykinin Antagonism
MEN 10207 has been used to block NKA-mediated responses in recombinant receptor and smooth-muscle systems. Its pharmacological profile is substantially different from the agonist behavior of native Neurokinin A.
Published potency values are assay-specific and should be treated as reference pharmacology rather than batch specifications.
A Direct SAR Partner for NKA (4-10)
Because both molecules contain seven residues, comparing MEN 10207 with NKA (4-10) provides a compact system for examining how stereochemistry, aromaticity and C-terminal charge can convert an agonist-derived scaffold into an antagonist.
Frequently Asked Questions
Is MEN 10207 an NK2 agonist?
No. It is primarily characterized as an NK2-selective peptide antagonist.
Why are the D-Trp residues important?
Experimental substitution studies showed that the three D-Trp residues collectively contribute strongly to affinity and selectivity.