pe
pep-10611 v1 CC-BY-SA-4.0

26RFa brain-signaling peptide

A naturally occurring neuropeptide that activates a poorly understood brain receptor (SP9155); studied only in lab experiments, not yet a drug.

statussynthesized targetOPRM1 length9 aa refs1
status 4 / 5
prediction metrics boltz-2 1.0
ipTM0.942
pTM0.806
avg pLDDT78.4
ranking score0.815
STRUCTURE · PEP-10611 × OPRM1
ranking0.815
target interface 4.5Å peptide drag rotate · ctrl+scroll zoom · right-click pan
boltz-2 1.0 · mmCIF ↓ download
sequence9 aa
159
KKGGFSFRF
overview readme

Snapshot

Class: Endogenous RFamide neuropeptide ligand
Evidence tier: In vitro / assay evidence
Status: Research peptide; no approved therapeutic status identified
Best-supported effect: Receptor binding and activation of orphan GPCR SP9155 in characterization assays (in vitro)
Main caveat: Evidence is limited to the original receptor-identification study; no animal or human data identified


What this is

P517 (KKGGFSFRF-NH2) is a 9-residue RFamide peptide of human origin identified as a ligand for the orphan G-protein-coupled receptor SP9155. It was characterized in a 2003 receptor-deorphanization study and belongs to the broader RFamide neuropeptide family, which shares the conserved C-terminal Arg-Phe-NH2 motif. No therapeutic application, animal efficacy model, or human study is identifieds available literature.


Evidence map

Evidence layerGradeWhat it supports
HumanNone identifiedNo human trial or observational evidence is identifieds available literature
AnimalNone identifiedNo animal experiment evidence is identifieds available literature
In vitroWeakReceptor identification and ligand characterization for SP9155 in cell-based assays (Jiang et al. 2003)
ComputationalNone identifiedNo computational or structural prediction data is identifieds available literature
MechanismPlausibleRFamide GPCR agonism inferred from receptor-identification assay results; downstream pathway not characterized in attached source

Claim check

ClaimVerdictEvidence layerConfidence
Binds and activates orphan GPCR SP9155Supported (in vitro)In vitroMedium — single characterization study; no independent replication identified in source
Any therapeutic or physiological role in humansNot establishedNoneLow — no human, animal, or mechanistic downstream data identifieds available literature
Receptor selectivity beyond SP9155Not establishedNoneLow — selectivity profile not described in attached source

Assay conditions

This section reports conditions used in the receptor-identification assay. It does not establish animal or human exposure.

ContextSystemAssay conditionTimepointEndpointLimitation
Orphan GPCR characterizationCell-based receptor assay (SP9155-expressing cells)Peptide applied at assay concentrations; exact concentration not extracted from sourceNot specified in sourceReceptor binding and activation of SP9155Single study; no independent replication identified; conditions not individually extracted

Assay limitations

  • Evidence is derived from a single receptor-identification and characterization study; independent replication is not present.
  • No animal toxicology or human safety data are identified.
  • In vitro receptor activity does not establish systemic tolerability, bioavailability, or physiological relevance.
  • The downstream signaling pathways activated by SP9155 following P517 binding are not characterized in the attached source.

Mechanism

P517 acts as a ligand for SP9155, an orphan G-protein-coupled receptor. The RFamide C-terminal motif (Arg-Phe-NH2) is shared across the RFamide neuropeptide family and is generally associated with GPCR recognition, though the specific signaling cascade downstream of SP9155 activation is not described in available literature. The receptor target is verified by the characterization study; the broader physiological or pharmacological significance of this interaction remains uncharacterized in the attached source.


Chemistry

FieldValue
Amino-acid chainKKGGFSFRF
Full IUPAC notationH-Lys-Lys-Gly-Gly-Phe-Ser-Phe-Arg-Phe-NH2
Length9 amino acids
TopologyLinear
C-terminal modificationAmidation (–NH2)
Species of originHuman (Homo sapiens)
Molecular weightNot extracted from source
FormulaNot extracted from source
CASNot extracted from source
Sequence confidenceNeeds review — source is single catalog entry; not cross-checked against primary sequence databases in this card

Open questions

  • Physiological role: The biological function of P517 and SP9155 in human physiology has not been characterized in the attached source. What tissue or circuit context is relevant?
  • Receptor deorphanization completeness: SP9155 is described as an orphan GPCR; whether it has since been fully characterized or renamed is not addressed in the attached source.
  • Selectivity profile: Whether P517 is selective for SP9155 over other RFamide receptors (e.g., NPFF receptors, QRFP receptor) is not established in the attached source.
  • Downstream signaling: The G-protein coupling and intracellular signaling pathway activated by SP9155 upon P517 binding are not described.
  • Animal and human translation: No animal model or human evidence is identified; whether the receptor interaction has physiological or pharmacological significance in vivo is unknown.
Hypotheses5 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 2026-06-05

Is KKGGFSFRF actually acting on opioid receptors, or does it target a different family of brain receptors that modify how opioids work?

Getting the receptor right changes the entire drug development strategy: if this peptide modifies opioid signaling indirectly, it could be developed to reduce opioid side effects like tolerance and addiction without being an opioid itself, which would be highly valuable clinically.

The hypothesis
The annotation of KKGGFSFRF to OPRM1 (mu-opioid receptor) is likely incorrect: the conserved C-terminal Arg-Phe motif identifies this peptide as an RFamide, a family that acts primarily at neuropeptide FF receptors (NPFFR1, NPFFR2) and QRFPR, not at opioid receptors, and the high ipTM (0.942) against OPRM1 may reflect the general hydrophobic-aromatic character of the C-terminal Phe docking into the opioid receptor's hydrophobic binding pocket without constituting a true agonist interaction.
Why it’s plausible
The readme explicitly identifies P517/KKGGFSFRF as an RFamide peptide ligand for orphan GPCR SP9155 (Jiang et al., 2003). RFamide peptides ending in -RFa characteristically bind NPFFR1, NPFFR2, QRFPR, and related GPCRs. OPRM1 annotation may derive from the broadly documented opioid-modulating activity of RFamide peptides as allosteric modulators or functional antagonists, which is mechanistically distinct from direct agonism. The sequence KKGGFSFRF lacks the Tyr residue that anchors most opioid receptor ligands.
Why it matters
If KKGGFSFRF acts at NPFFR2 rather than OPRM1 directly, its pharmacological profile is that of an opioid-modulating anti-opioid peptide rather than an opioid agonist, fundamentally changing its potential therapeutic application from pain treatment to opioid side-effect management or addiction.
Plausibility.80
Novelty.50
Impact.75
Basis · grounding3 computed/notes
[1]
notereadme_excerpt identifies this peptide as an RFamide neuropeptide ligand for orphan GPCR SP9155 (Jiang et al. 2003); RFamide family members primarily act at NPFFR1/NPFFR2/QRFPR.
[2]
sequenceKKGGFSFRF: C-terminal -RF is the conserved RFamide motif; the peptide lacks Tyr at the N-terminus, which is required for OPRM1 agonism in classical opioid peptides (YGGFM in Met-enkephalin).
[3]
structureipTM=0.9417 against OPRM1; the high score may reflect Phe docking into the hydrophobic OPRM1 pocket without genuine agonist pharmacophore engagement.
openupdated 2026-06-05

Could this small neuropeptide fragment activate the brain receptor that triggers hunger and food-seeking behavior?

If this peptide activates the hunger-regulating QRFPR receptor, it could provide a minimal scaffold for developing treatments for conditions where stimulating appetite is critical, such as cancer-related weight loss, chemotherapy-induced anorexia, or wasting diseases.

The hypothesis
KKGGFSFRF, as an RFamide peptide with the conserved -RF C-terminus, could modulate feeding behavior and energy homeostasis via QRFPR (GPR103), the receptor for 26RFa/QRFP, because the peptide's C-terminal pentapeptide FSFRF overlaps with the minimal QRFPR-active sequence and the diLys N-terminus enhances cell membrane affinity in hypothalamic neurons where QRFPR is expressed.
Why it’s plausible
The readme names this peptide '26RFa brain-signaling peptide,' directly linking it to the 26RFa/QRFP neuropeptide system. 26RFa is an orexigenic peptide that stimulates food intake via QRFPR. The sequence KKGGFSFRF shares the C-terminal RFa motif and the Phe-Ser-Phe aromatic cluster that is part of the minimal QRFPR binding sequence. If this fragment has QRFPR activity, it represents a structurally minimal orexigenic probe.
Why it matters
A 9-residue QRFPR-active peptide derived from the 26RFa precursor would be the shortest known orexigenic RFamide fragment, with potential utility for studying hypothalamic feeding circuits and as a lead for treating anorexia or cachexia associated with cancer and chronic illness.
Plausibility.70
Novelty.50
Impact.65
Basis · grounding3 computed/notes
[1]
notePeptide is named '26RFa brain-signaling peptide' in the card title, directly connecting it to the QRFP/26RFa orexigenic neuropeptide system and QRFPR.
[2]
sequenceKKGGFSFRF: C-terminal FSFRF contains the Phe-Ser-Phe aromatic motif and the conserved -RF terminus; this overlaps with the minimal active sequence of 26RFa analogs reported in QRFPR pharmacology.
[3]
structureipTM=0.9417 against OPRM1 is high, but the opioid receptor annotation is questionable (see target-binding hypothesis); QRFPR docking of the same sequence may yield equal or higher confidence.
openupdated 2026-06-05

Does the serine in the middle of this peptide make it selectively activate one hunger-regulating brain receptor rather than the pain-signaling receptors in the same family?

A peptide that selectively activates QRFPR without activating NPFF receptors could be used to study appetite regulation without confounding effects on pain and opioid signaling, and could potentially be developed into a more targeted drug for metabolic or eating disorders.

The hypothesis
The Phe-Ser-Phe (FSF) motif at positions 5-7 of KKGGFSFRF confers selectivity for SP9155/QRFPR over NPFFR1 and NPFFR2, because NPFF receptors prefer peptides with a Leu or Pro preceding the terminal RF, while QRFPR tolerates Phe at this position, and the Ser hydroxyl at position 6 could make a polar contact unique to the QRFPR binding pocket.
Why it’s plausible
Among RFamide receptor subtypes, NPFFR1 and NPFFR2 preferentially bind peptides with the sequence motif xLRFa or xPQRFa, while QRFPR binds 26RFa with the distal sequence ...FSLRFa. The FSF motif in KKGGFSFRF differs from both canonical sequences but is more similar to the QRFPR-preferred Phe-containing motifs. The Ser at position 6 is a potential selectivity determinant because NPFF receptors' binding pockets are more hydrophobic at equivalent positions.
Why it matters
If KKGGFSFRF is QRFPR-selective over NPFFR subtypes, it would represent a useful pharmacological tool for dissecting RFamide receptor subtype contributions to feeding, pain, and neuroendocrine regulation, where the lack of selective ligands is a major research limitation.
Plausibility.50
Novelty.55
Impact.60
Basis · grounding3 computed/notes
[1]
sequenceKKGGFSFRF: positions 5-7 are Phe-Ser-Phe; the Ser hydroxyl and Phe-Phe flanking are distinct from the Leu/Pro-containing motifs preferred by NPFFR1/NPFFR2.
[2]
notereadme_excerpt identifies SP9155 as the characterized target in the original deorphanization study (Jiang et al. 2003); SP9155 corresponds to QRFPR in current nomenclature.
[3]
structureipTM=0.9417 against OPRM1 (questionable annotation); if the true receptor is QRFPR, the structural basis for selectivity within the RFamide family requires analysis against all RFamide receptor subtypes.
openupdated 2026-06-05

Do the two positively charged amino acids at the front of this peptide help it concentrate near cell surfaces, making it more potent at activating its receptor?

If the membrane-anchoring role of the diLysine is confirmed, drug designers could engineer more potent analogs by tuning this electrostatic patch, potentially leading to lower effective doses of any therapeutic derived from this peptide family.

The hypothesis
The N-terminal diLys (KK) motif in KKGGFSFRF functions as a membrane-anchoring electrostatic patch that concentrates the peptide at negatively charged plasma membranes prior to receptor engagement, reducing the effective EC50 at its cognate GPCR (SP9155/QRFPR family) by a pre-concentration mechanism analogous to that described for other cationic neuropeptides.
Why it’s plausible
Cationic N-terminal residues in neuropeptides (e.g., KK, RR) are known to mediate electrostatic association with anionic membrane phospholipids, creating a local two-dimensional concentration effect that enhances GPCR encounter probability. The two Lys residues at the N-terminus of KKGGFSFRF add a net charge of +2 that would drive membrane association at physiological pH. This is mechanistically separable from receptor binding per se.
Why it matters
If the KK motif provides a membrane pre-concentration function, truncated analogs lacking the N-terminal Lys residues would show dramatically reduced potency at the target receptor despite similar intrinsic binding affinity, explaining why full-length RFamide peptides are required for physiological activity even when the C-terminal -RF motif is sufficient for receptor recognition in vitro.
Plausibility.60
Novelty.45
Impact.50
Basis · grounding3 computed/notes
[1]
sequenceKKGGFSFRF: positions 1-2 are Lys-Lys (diLys), net charge +2 at pH 7; positions 3-4 are Gly-Gly (flexible linker); C-terminal FSFRF contains the RFamide pharmacophore.
[2]
structurepLDDT=78.4 is moderate, consistent with a flexible N-terminal KK segment and a more ordered C-terminal RFamide segment, compatible with the proposed membrane-anchor/pharmacophore domain architecture.
[3]
notereadme_excerpt notes the conserved C-terminal Arg-Phe-NH2 motif as defining the RFamide family, implying the N-terminal portion is variable and may have auxiliary rather than primary receptor-binding roles.
openupdated 2026-06-05

Does the flexible middle section of this peptide act as a joint that allows the pharmacophore end to swing into different receptor-binding positions?

If the glycine hinge controls receptor selectivity, chemists could design modified versions with a rigid hinge that preferentially activate the appetite receptor rather than pain receptors, providing more targeted drugs with fewer side effects for metabolic disorders.

The hypothesis
The Gly-Gly (GG) dipeptide at positions 3-4 of KKGGFSFRF acts as a conformationally flexible hinge that allows the N-terminal KK electrostatic anchor and the C-terminal FSFRF pharmacophore to adopt independent orientations, and substituting this GG hinge with a single Pro would rigidify the peptide backbone and shift receptor subtype selectivity by forcing the pharmacophore into a constrained presentation geometry.
Why it’s plausible
Gly residues confer maximum backbone flexibility (no side chain, minimal steric restriction). A diGly hinge between two functional domains (KK and FSFRF) would allow the pharmacophore to swivel freely relative to the membrane anchor. Pro substitution at position 3 or 4 would introduce a fixed kink. RFamide receptor binding is sensitive to N-terminal extension conformation in multiple published structure-activity studies on NPFF and related peptides.
Why it matters
If the GG hinge is a conformational gate for receptor subtype selectivity, Pro-substituted KKGGFSFRF analogs could preferentially activate one RFamide receptor subtype over others, providing novel selective pharmacological probes for dissecting the overlapping roles of RFamide receptors in pain, appetite, and neuroendocrine function.
Plausibility.50
Novelty.55
Impact.55
Basis · grounding3 computed/notes
[1]
sequenceKKGGFSFRF: positions 3-4 are Gly-Gly; this is the most flexible possible linker between the diLys anchor (positions 1-2) and the FSFRF pharmacophore (positions 5-9).
[2]
structurepLDDT=78.4 overall; the Gly-Gly region is expected to contribute to lower local confidence, consistent with high flexibility at positions 3-4.
[3]
notereadme_excerpt states that downstream pathway characterization was not performed in the original study, leaving the structural basis for receptor activation undefined; hinge flexibility is an unexplored structural variable.
details expand to inspect
full evidence table2 metrics
metricvaluetool
ipTM 0.9417022466659546 boltz-2
ranking score 0.8153480887413025 boltz-2
structural qualityopenfold3
metricvaluenote
gpde1.064global PDE — lower = better
disorderNaNfraction disordered
3-letter notation
Lys-Lys-Gly-Gly-Phe-Ser-Phe-Arg-Phe
recipeboltz-2 1.0
parametervalue
modelboltz-2 1.0
weights
hardwarenvidia_nim_api
mlx version
python
random seed
msa strategynone
diffusion samples1
runtime
predicted bymlx@peptide
predicted at2026-04-24
citationbibtex
peptidemodel (2026). 26RFa brain-signaling peptide (pep-10611, v1). PeptideModel. https://peptidemodel.com/card/pep-10611
@peptide{pep10611,
  sequence = {KKGGFSFRF},
  target   = {oprm1},
  author   = {peptidemodel},
  year     = {2026},
  status   = {synthesized}
}
related peptides 1 by signal overlap
clinical trials 0 trials · checked 2026-05-09
0
no registered clinical trials as of 2026-05-09; we'll re-check periodically
references 1 papers
discussion no comments
sign in to comment
peptidemodel.com CC-BY-SA-4.0 research only · not for human use