pe
pep-10446 v1 CC-BY-SA-4.0

Substance P receptor activator (CHEMBL1651026)

A lab-made peptide that switches on the substance P receptor, a signal involved in pain and inflammation; used only as a research tool.

statusbioassayed targetTACR1 length9 aa refs5
status 5 / 5
prediction metrics boltz-2 2.2.1
ipTM0.879
pTM0.821
avg pLDDT72.4
ranking score0.755
STRUCTURE · PEP-10446 × TACR1
ranking0.755
target interface 4.5Å peptide drag rotate · ctrl+scroll zoom · right-click pan
boltz-2 2.2.1 · mmCIF ↓ download
sequence9 aa
159
RPKPQQFFL
in the news 1 article
overview readme

What this is

CHEMBL1651026 is a synthetic nine-residue research peptide derived from the C-terminal "message" region of substance P, designed as a highly potent, NK1-selective agonist of the tachykinin NK1 receptor (TACR1). The stored sequence RPKPQQFFL is a standard-letter approximation of an analog in the well-characterized [Sar9,Met(O2)11]-substance P family — research-grade reference ligands that swap Gly9 for sarcosine (N-methyl-glycine) and oxidize the C-terminal Met11 to a methionine sulfone, with the carboxyl group amidated. Neither the sarcosine substitution, the methionine oxidation, nor the C-terminal amide is captured by the 1-letter code; they are what make the molecule resistant to proteolysis and selective for NK1 over NK2/NK3. The compound is a chemical tool used in receptor pharmacology and ligand-discovery screens — not a clinical drug.

History

The parent peptide, substance P, was the first peptide ever described in the modern neuropeptide era: von Euler and Gaddum (1931) extracted a smooth-muscle-contracting "preparation" (the "P" of substance P) from horse brain and intestine at the National Institute for Medical Research in London. Forty years later, Chang, Leeman and Niall (Nature New Biology, 1971) purified the active material from bovine hypothalamus and sequenced it as the undecapeptide Arg-Pro-Lys-Pro-Gln-Gln-Phe-Phe-Gly-Leu-Met-NH₂. Replacing Gly9 with sarcosine and oxidizing Met11 to its sulfone yielded [Sar9,Met(O2)11]-substance P, which became a standard radioligand-grade NK1 agonist after autoradiographic mapping studies in the late 1980s and early 1990s (Dam et al., Brain Research, 1990). CHEMBL1651026 sits within this class as one of several truncated or sarcosine-substituted analogs catalogued by the ChEMBL bioactivity database.

What it does

The molecule binds with sub-nanomolar affinity to the human NK1 receptor and activates it as an agonist. ChEMBL records report IC50 values of 0.11 nM in displacement binding assays against human NK1 (with additional values from related assays ranging 0.14–2.1 nM depending on the format). NK1 is a Gαq- and Gαs-coupled G-protein-coupled receptor expressed in the central nervous system, dorsal-horn spinal neurons, and immune and gut tissue; its endogenous ligand, substance P, is the principal neurotransmitter mediating neurogenic inflammation, pain transmission, and nausea/emesis signaling (Steinhoff et al., Physiological Reviews, 2014; Mantyh, Journal of Clinical Psychiatry, 2002). As a selective agonist, CHEMBL1651026 mimics substance P at NK1 with minimal cross-activity at NK2 (tachykinin neurokinin A receptor) or NK3 (neurokinin B receptor) — the basis of its use as a pharmacological tool.

Mechanism

NK1 belongs to the Family A (rhodopsin-like) GPCR superfamily. Cryo-electron microscopy structures of human NK1 in complex with substance P and either Gq or Gs heterotrimers show the C-terminal "message" region of substance P (positions 6–11, FFGLM-NH₂) inserted deep into the orthosteric pocket between transmembrane helices 3, 5, 6 and 7, while the N-terminal "address" region (positions 1–4, RPKP) extends out toward the extracellular vestibule and helps define receptor subtype selectivity (Thom et al., Science Advances, 2021). Truncating substance P to its C-terminal 6–8 residues retains NK1 agonism but loses NK1 selectivity; the full N-terminal address sequence — Arg-Pro-Lys-Pro — that this analog retains is the structural feature that keeps it NK1-selective against NK2/NK3. The Sar9 substitution removes the only proteolytically labile peptide bond in the message region (Gly-Leu) and the Met(O2)11 modification blocks oxidative inactivation of the C-terminal methionine, together extending plasma stability without disrupting receptor engagement. Substance-P-class agonists at NK1 are biased toward distinct Gq-versus-β-arrestin signaling outputs depending on residue substitutions in the message region (Harris et al., Nature Chemical Biology, 2021).

Evidence

  • In vitro: Radioligand-displacement and functional NK1 binding assays — IC50 0.11 nM, Ki 0.14 nM at human NK1 receptor across multiple published assay reports indexed in ChEMBL under CHEMBL1651026.
  • Animal: The broader [Sar9,Met(O2)11]-substance P class has been used as a tool agonist in rodent models of neurogenic inflammation, nociception, and emesis; no animal pharmacology has been published for the specific CHEMBL1651026 analog itself.
  • Human: No human trials. This is a research-grade chemical tool, not a clinical candidate.

Regulatory status

  • US: Not an approved drug; not in clinical development. Available only as a research chemical.
  • EU: Not an approved drug; not in clinical development.
  • WADA: Not specifically listed. Substance-P agonists as a class have no anti-doping relevance.

For context, the NK1 receptor antagonist class — the opposite pharmacology — has produced several FDA-approved drugs for chemotherapy-induced nausea and vomiting, including aprepitant (Emend, approved 2003), fosaprepitant (Emend IV, approved 2008), and rolapitant (Varubi, approved 2015). CHEMBL1651026 is an agonist and is unrelated to these therapeutics.

Related peptides

The closest family member already on the platform is the endogenous parent peptide, substance P (Arg-Pro-Lys-Pro-Gln-Gln-Phe-Phe-Gly-Leu-Met-NH₂), and the other endogenous mammalian tachykinins (neurokinin A, neurokinin B) that share the C-terminal FXGLM-NH₂ message motif but engage NK2 and NK3 in preference to NK1 (Steinhoff et al., 2014). NK1-receptor-targeting research analogs in this series differ chiefly in N-terminal truncation, single-residue substitutions, and C-terminal amide chemistry.

Hypotheses3 directions▾ collapse

Research directions for this peptide, selected from the current sources — hypotheses you can explore and model. None of it is proven yet; tap any one to see the full thinking.

openupdated 2026-06-11

Does this card store a stripped 9-residue version that is missing the chemical modifications and C-terminal amide of the actual ChEMBL ligand?

The 0.11 nM potency on this card belongs to the full modified analog (sarcosine, methionine-sulfone, amidated C-terminus), not to the bare RPKPQQFFL stored here. Anyone using the stored sequence as an NK1 reference could badly overestimate its activity. Flagging the mismatch protects NK1 screening data.

The hypothesis
The unmodified RPKPQQFFL sequence, lacking sarcosine at position 9 and the C-terminal amide, adopts a distinct backbone conformation at the C-terminus compared to [Sar9,Met(O2)11]-substance P, reducing its intrinsic NK1 agonist potency by at least one order of magnitude relative to the parent analog despite preserving the core pharmacophore residues.
Why it’s plausible
The Sar9 substitution in the parent analog eliminates the Gly9 NH, restricting backbone flexibility and enforcing a beta-turn geometry critical for high-affinity NK1 engagement. RPKPQQFFL retains Gly-equivalent flexibility at that position (Phe replaces Gly9 here, actually), and lacks the C-terminal amide that removes a negative charge. These two modifications together in the parent are known to raise potency; their absence should quantifiably lower it.
Why it matters
If true, the stored sequence is a lower-potency surrogate, meaning any screen using RPKPQQFFL as an NK1 reference agonist would systematically underestimate target activation, misranking test compounds relative to clinical benchmarks.
Plausibility.85
Novelty.60
Impact.85
Basis · grounding2 computed/notes
[1]
noteREADME explicitly states sarcosine at 9 and Met sulfone at 11 and C-terminal amide are NOT captured by the 1-letter code and are what confer potency and selectivity
[2]
sequenceRPKPQQFFL ends in Leu with a free carboxyl; no indication of amidation in the stored sequence
openupdated 2026-06-11

Does the Arg-Pro-Lys prefix act as a docking guide that speeds binding rather than tightening grip?

Substance P is known to have a two-part design: a positively charged N-terminal 'address' that steers it to the receptor and a C-terminal 'message' that activates it. If the address mainly speeds up binding, designers could tune it to control how fast NK1 drugs act, which matters for emergency pain or nausea care. (This rests on the established two-domain model, not on any structure prediction for this specific card.)

The hypothesis
The RPK motif at the N-terminus of RPKPQQFFL enables electrostatic pre-docking to negatively charged extracellular loop residues of TACR1, acting as an address sequence that increases the local concentration of the C-terminal message pharmacophore (QQF/FL) at the binding site, such that removing or scrambling the RPK segment would disproportionately reduce association rate rather than equilibrium affinity.
Why it’s plausible
Substance P structure-activity studies have established a two-domain model: an N-terminal 'address' (RPK) directing the peptide to the receptor and a C-terminal 'message' (FGLM-NH2 or equivalent) responsible for activation. The relatively high ipTM=0.88 suggests a well-defined docked pose. If the address drives kon, disrupting it should slow binding kinetics more than it shifts IC50 at equilibrium.
Why it matters
Understanding whether the address affects kinetics versus affinity has direct implications for designing faster-acting or more slowly dissociating NK1 therapeutics, particularly for acute pain or antiemetic applications.
Plausibility.70
Novelty.70
Impact.60
Basis · grounding3 computed/notes
[1]
structureboltz-2 complex ipTM=0.8787 suggests a confident docked pose, consistent with a well-organized two-domain binding mode
[2]
sequenceRPKPQQFFL starts with Arg-Pro-Lys, a strongly cationic address segment, followed by the hydrophobic C-terminal message residues
[3]
noteREADME describes the peptide as derived from the C-terminal message region of substance P, implying address-message duality is relevant
openupdated 2026-06-11

Could the stored sequence, lacking the modifications and C-terminal amide of the real ligand, show activity at NK2 and NK3 rather than being NK1-selective?

Tachykinin-receptor selectivity comes mostly from the peptide's makeup as a whole, so a degraded fragment may behave very differently from the intended NK1-selective compound. Confirming this would prevent misreading pain, nausea, or inflammation results obtained with the stored sequence. (Note: selectivity is driven more by the overall sequence than by the sarcosine and sulfone groups alone, so the premise is worth testing but not assured.)

The hypothesis
RPKPQQFFL, without the modifications that differentiate [Sar9,Met(O2)11]-substance P from native substance P, retains cross-reactivity toward NK2 (TACR2) and NK3 (TACR3) receptors at concentrations used in typical cell-based assays (100 nM to 1 uM), undermining its use as an NK1-selective tool compound.
Why it’s plausible
NK1 selectivity in the [Sar,Met(O2)] series depends critically on the sarcosine and sulfone modifications. The RPKPQQFFL sequence is essentially a truncated substance P C-terminal fragment, and such fragments show measurable NK2/NK3 activity at higher concentrations. If selectivity is lost, any phenotypic readout attributed to NK1 may partly reflect NK2/NK3 signaling.
Why it matters
NK1, NK2, and NK3 have distinct physiological roles. Misattributing a biological effect to NK1 alone, when the unmodified sequence activates all three, could invalidate mechanistic conclusions about nociception, neuroinflammation, or emesis models.
Plausibility.45
Novelty.55
Impact.50
Basis · grounding2 computed/notes
[1]
noteREADME states that the sarcosine and sulfone modifications are what make the molecule selective for NK1 over NK2/NK3; these are absent in the stored sequence
[2]
sequenceRPKPQQFFL corresponds to residues 1-9 of substance P without modifications, a fragment known from literature to retain some panreceptor activity
details expand to inspect
full evidence table1 metrics
metricvaluetool
IC50 0.11 nM GPCRDB/ChEMBL
3-letter notation
Arg-Pro-Lys-Pro-Gln-Gln-Phe-Phe-Leu
recipeboltz-2 2.2.1
parametervalue
modelboltz-2 2.2.1
weights
hardwarevast_v100_32gb
mlx version
python
random seed1
msa strategycolabfold_local
runtime
predicted by
predicted at2026-05-22
citationbibtex
peptidemodel (2026). Substance P receptor activator (CHEMBL1651026) (pep-10446, v1). PeptideModel. https://peptidemodel.com/card/pep-10446
@peptide{pep10446,
  sequence = {RPKPQQFFL},
  target   = {tacr1},
  author   = {peptidemodel},
  year     = {2026},
  status   = {bioassayed}
}
related peptides 4 by signal overlap
clinical trials 0 trials · checked 2026-05-22
0
no registered clinical trials as of 2026-05-22; we'll re-check periodically
references 5 papers
discussion no comments
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peptidemodel.com CC-BY-SA-4.0 research only · not for human use