pe
pep-04486 v1 CC-BY-SA-4.0

Brain hunger-signaling peptide (Neuropeptide W-23)

A natural brain signaling molecule that stimulates appetite and may regulate body weight; discovered in 2002 and used only as a lab research tool.

statusbioassayed targetNPBWR1 length23 aa refs3
endogenous
status 2 / 5 · 0 verified on platform
prediction metrics boltz-2 2.2.1
ipTM0.938
pTM0.922
avg pLDDT84.3
ranking score0.862
STRUCTURE · PEP-04486 × NPBWR1
ranking0.862
target interface 4.5Å peptide drag rotate · ctrl+scroll zoom · right-click pan
boltz-2 2.2.1 · mmCIF ↓ download
sequence23 aa
1510152023
WYKHVASPRYHT VGRAAGLLMGL
overview readme

What this is

Neuropeptide W-23 (NPW-23) is a short signaling molecule made naturally in the brain. It belongs to a two-peptide family — NPW-23 and its slightly longer sibling NPW-30 — both produced from the same precursor gene (prepro-NPW) through proteolytic cleavage. The name "W" comes from the tryptophan residues (single-letter code W) that flank both the N- and C-termini of the mature peptide. NPW-23 was isolated from porcine hypothalamus in 2002 by Shimomura and colleagues at Takeda Chemical Industries (Shimomura 2002) and has no approved clinical use.

History

NPW-23 was discovered in 2002 through a reverse-pharmacology strategy: Shimomura and colleagues exposed Chinese Hamster Ovary (CHO) cells expressing two orphan G-protein-coupled receptors — GPR7 and GPR8 — to porcine hypothalamic extracts, monitoring inhibition of forskolin-induced cAMP production as a readout of receptor activation (Shimomura 2002). This screen identified NPW as the endogenous ligand for both receptors. The receptors were subsequently renamed NPBWR1 (GPR7) and NPBWR2 (GPR8) to reflect their shared ligand family with the related Neuropeptide B. A year later, Ishii, Fei, and Friedman at Rockefeller University showed that male mice with a targeted disruption of the GPR7 gene develop progressive adult-onset obesity, placing NPW-23 and its receptor into the expanding network of hypothalamic energy-balance regulators (Ishii 2003).

What it does

NPW-23 is a neuromodulator with effects on appetite, stress hormones, pain signaling, and cardiovascular tone — all principally studied through central (brain) administration in rodents. Intracerebroventricular (i.c.v.) infusion in rats elevates plasma corticosterone and activates the hypothalamic–pituitary–adrenal (HPA) axis via corticotropin-releasing factor (CRF) neurons in the paraventricular nucleus (Mondal 2003; Sakurai 2013). Central NPW administration also transiently increases food intake in fasted or light-phase rats, while sustained infusion suppresses feeding; conversely, immunoneutralisation of endogenous NPW with anti-NPW antibodies stimulates feeding, indicating that endogenous NPW tonically restrains appetite in certain contexts (Mondal 2003; Sakurai 2013). Intrathecal NPW-23 reduces inflammatory pain responses in rodent models without engaging opioid receptors, suggesting an independent spinal analgesic pathway (Dvorakova 2018). Centrally administered NPW also increases mean arterial blood pressure, heart rate, and plasma catecholamine concentrations in rats, while peripheral vascular studies show NPW-23 modulates the Cav1.2 L-type calcium channel current in vascular smooth muscle cells via NPBWR1 and the PLC/PKC pathway, contributing to arterial tone (Li Ji 2015).

Evidence

  • Human: No human intervention trials for NPW-23 have been published. One registered trial (vagus nerve stimulation in systemic lupus erythematosus) measures circulating NPW as an exploratory biomarker but does not administer the peptide. No registered trials on ClinicalTrials.gov involve NPW-23 as a therapeutic agent.
  • Animal: Male GPR7 (NPBWR1) knockout mice develop progressive adult-onset obesity with hyperphagia and decreased energy expenditure; female knockouts do not show the same phenotype, indicating sex-specific regulation (Ishii 2003). Exogenous NPW-23 administered i.c.v. elevates corticosterone and activates CRF neurons in rat PVN; CRF antagonist pretreatment blocks this effect (Mondal 2003; Sakurai 2013). Intrathecal NPW-23 suppresses Fos-like immunoreactivity in the spinal dorsal horn during inflammatory pain (Dvorakova 2018).
  • In vitro: NPW-23 inhibits forskolin-stimulated cAMP production in CHO cells expressing NPBWR1 or NPBWR2, consistent with Gi-coupled signalling (Shimomura 2002). In rat vascular smooth muscle cells, NPW-23 stimulates PKC phosphorylation, elevates diacylglycerol, and modulates Cav1.2 current via GPR7 (Li Ji 2015).

Known effects

  • Appetite modulation — Context-dependent (acute orexigenic; sustained or endogenous tone anorexigenic); Preclinical
  • HPA axis activation — Elevates plasma corticosterone via CRF; Preclinical
  • Inflammatory pain reduction — Intrathecal; opioid-independent; Preclinical
  • Cardiovascular regulation — Increases blood pressure and heart rate (central); modulates vascular smooth muscle Cav1.2 current (peripheral); Preclinical
  • Neuroendocrine effects — Stimulates prolactin; inhibits growth hormone; Preclinical

Safety signals

No human safety data exist for exogenous NPW-23 administration. All published evidence comes from rodent pharmacology. The obesity phenotype observed in male NPBWR1 knockout mice (Ishii 2003) suggests that chronic disruption of NPW signalling has metabolic consequences, though the direction of effect (loss vs. gain of NPW activity) remains a subject of investigation given the context-dependent feeding effects.

Regulatory status

  • US: Not approved. No IND or clinical development programme identified.
  • EU: Not approved.
  • Research use: Investigational tool compound only; used in receptor pharmacology, neuroendocrinology, and pain research.

Mechanism

NPW-23 is the 23-residue N-terminal fragment of the 30-residue precursor NPW-30, generated by proteolytic cleavage at a pair of arginine residues at positions 24–25 of prepro-NPW; NPW-23 and NPW-30 are both biologically active, with NPW-23 showing slightly higher potency at NPBWR1 and NPBWR2 (Sakurai 2013). Both receptors couple to inhibitory Gi-class G-proteins, suppressing adenylyl cyclase (cAMP inhibition) and activating GIRK (Kir3) potassium channels; the Gβγ subunit additionally stimulates ERK (p42/p44) activity (Sakurai 2013). NPBWR2 (GPR8) is notably absent from the rodent genome, being expressed only in humans, rabbits, and certain other mammals, making rodents a model for NPBWR1 signalling only (Dvorakova 2018; Singh and Davenport 2006).

NPW-producing cell bodies in rodent brain are restricted to a few midbrain and brainstem nuclei — the Edinger–Westphal nucleus, ventral tegmental area, periaqueductal grey, and dorsal raphe — but their axons project broadly to the extended amygdala (central amygdala and bed nucleus of the stria terminalis), which express the highest levels of NPBWR1 mRNA (Sakurai 2013). The concentration of NPW inputs to limbic structures controlling stress and emotion, alongside the obesity and anxiety-related phenotypes of NPBWR1 knockout animals, positions NPW-23 as a hypothalamic–limbic integrator linking nutritional status, stress, and affect (Sakurai 2013; Dvorakova 2018).

In the periphery, NPW mRNA is expressed in gastric antral G cells, pancreatic islets, adrenal cortex and medulla, thyroid, testes, ovary, kidney, and lung; gastric NPW levels fall during fasting and rise after refeeding, consistent with a nutritional-state sensor role (Dvorakova 2018).

Open questions

  • The opposing orexigenic and anorexigenic effects of acute versus sustained central NPW administration remain mechanistically unexplained
  • NPBWR2's absence in rodents means that human NPW-23 pharmacology — where both receptors are expressed — may differ substantially from rodent predictions
  • A human NPBWR1 polymorphism (rs33977775, 404A>T, Y135F within the conserved DRY motif) shows partially impaired cAMP inhibition and altered emotional responses to facial stimuli, but its metabolic phenotype in humans has not been characterised (Sakurai 2013)
  • No selective NPBWR1 agonists or antagonists have advanced to clinical testing
  • Whether circulating or CSF NPW levels are altered in human obesity, anxiety disorders, or chronic pain remains unstudied

Related peptides

  • Neuropeptide B (NPB) — the closest structural relative; shares NPBWR1/NPBWR2 as ligands and overlapping CNS effects; NPB29 shows selective preference for NPBWR1 (EC50 ~0.23 nM) vs NPBWR2 (EC50 ~15.8 nM), distinguishing it from the less-selective NPW-23 (Sakurai 2013)
  • NPW-30 — the longer isoform of the same gene; identical N-terminal sequence, slightly lower receptor potency than NPW-23
Hypotheses6 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

Could steady, low-level activation of the NPW brain receptor prevent obesity even though a single large dose seems to make animals eat more?

If confirmed, this would mean that drugs designed to gently sustain NPW receptor signaling could fight obesity rather than worsen it, opening an entirely new class of weight-loss therapies based on restoring a naturally occurring brake on overeating.

The hypothesis
Chronic central deficiency of NPBWR1 signaling, rather than excess, is the driver of the obesity phenotype in GPR7-knockout mice, meaning that NPBWR1 agonists based on NPW-23 would suppress hyperphagia and prevent adult-onset obesity without causing the anorexia seen after acute intracerebroventricular bolus dosing.
Why it’s plausible
Acute ICV injection of NPW promotes food intake and corticosterone release (Shimomura 2002; DOI 10.1210/en.2003-0536), yet GPR7-knockout mice become hyperphagic and obese (Ishii 2003, referenced in readme). This apparent paradox suggests that the acute feeding-stimulatory effect may reflect a rebound or stress-coupled mechanism, while tonic NPBWR1 signaling over days restrains adiposity. If chronic low-dose agonism recapitulates tonic signaling, it could be anti-obesity rather than pro-obesity.
Why it matters
Resolving this paradox is essential before any NPBWR1-targeting therapeutic program is initiated. If tonic agonism is anorexigenic, NPW-23 analogues become credible anti-obesity leads; if the acute effect dominates, they are contraindicated.
Plausibility.55
Novelty.70
Impact.80
Basis · grounding1 paper · 2 computed/notes
[1]
paper
Central NPW23 and NPW30 stimulate food intake and water drinking acutely; GPR7 knockout mice are hyperphagic and obese, creating a mechanistic paradox
doi: 10.1210/en.2003-0536
[2]
noteIshii 2003 showed male GPR7-knockout mice develop progressive adult-onset obesity, suggesting a tonic restraining role for the receptor
[3]
noteNPW-23 modulates HPA axis (corticosterone), which could confound acute feeding studies via stress-induced hyperphagia rather than direct orexigenic action
openupdated 2026-06-05

If you shorten or redesign NPW-23, can you keep its ability to reduce overeating while losing the side effect of raising cortisol?

A peptide that activates only the 'helpful' side of this receptor could treat obesity without the metabolic and immune consequences of chronically elevated stress hormones, making it far safer for long-term use in patients with weight-related conditions.

The hypothesis
NPW-23 exhibits tissue-level functional selectivity between the hypothalamus and the adrenal/pituitary axis through differential NPBWR1 coupling to Gi versus beta-arrestin pathways, such that biased agonists retaining the WYKHV N-terminal motif but lacking the C-terminal LLMGL segment would preferentially modulate energy balance while sparing corticosterone secretion.
Why it’s plausible
The readme notes NPW-23 affects both food intake/body weight and stress hormones (prolactin, corticosterone). These two outputs may involve different signaling branches downstream of NPBWR1: Gi-cAMP for hypothalamic circuit modulation versus beta-arrestin-mediated internalization and adrenal crosstalk. The N-terminal WYKHV contains charged and aromatic residues likely engaging the receptor binding pocket, while LLMGL at the C-terminus is a hydrophobic tail that could engage transmembrane helices differently. Biased agonism based on peptide truncation is established in other neuropeptide families.
Why it matters
Separating anorexigenic from corticosterone-elevating effects of NPBWR1 agonism is a prerequisite for a safe obesity drug; steroid elevation would cause metabolic and immunosuppressive side effects that would negate therapeutic benefit.
Plausibility.50
Novelty.75
Impact.75
Basis · grounding1 paper · 2 computed/notes
[1]
paper
NPW23 centrally elevates serum corticosterone and prolactin in addition to stimulating food intake, demonstrating pleiotropy downstream of NPBWR1
doi: 10.1210/en.2003-0536
[2]
sequenceWYKHV (positions 1-5): W aromatic anchor, Y hydroxyl, K cationic, H imidazole, V small hydrophobic; LLMGL (positions 19-23): purely hydrophobic, structural character distinct from N-terminal charged cluster
[3]
noteNPW-23 effects on cardiovascular tone reported alongside feeding and HPA effects, consistent with multiple effector pathways from a single receptor
openupdated 2026-06-05

Could an NPW-23-based drug reduce binge eating by calming the brain's stress response and appetite signals simultaneously through a single receptor?

Binge-eating disorder affects millions and has no drugs targeting its stress-eating root cause. If NPW-23 can address both stress hormones and appetite via one receptor, it could offer a new treatment option for people who eat compulsively in response to anxiety or trauma.

The hypothesis
NPW-23 or a stable analogue could suppress hypothalamic-pituitary-adrenal axis hyperactivation in stress-related eating disorders (binge-eating disorder, stress-induced obesity) by simultaneously dampening corticotropin-releasing factor circuit activity and modulating ghrelin-independent orexigenic drive via NPBWR1.
Why it’s plausible
NPW-23 is co-expressed with corticotropin-releasing factor (CRF) circuits in the hypothalamus and elevates corticosterone acutely, but GPR7-knockout obesity is associated with hyperphagia, suggesting that tonic NPW signaling normally restrains stress-coupled eating. Binge-eating disorder involves dysregulated HPA axis tone and stress-triggered food intake. If NPBWR1 agonism can attenuate the CRF-driven component of stress-induced hyperphagia while the receptor's energy-balance role normalizes baseline intake, the dual action could be uniquely suited to stress-eating phenotypes that do not respond to ghrelin pathway interventions.
Why it matters
Binge-eating disorder has no approved mechanistic pharmacotherapy targeting its stress-eating component; an NPBWR1-based approach would represent a genuinely novel mechanism of action distinct from GLP-1, ghrelin, and dopamine-based treatments currently under investigation.
Plausibility.50
Novelty.70
Impact.75
Basis · grounding2 papers · 1 computed/note
[1]
paper
Central NPW23 elevates corticosterone and stimulates food intake, demonstrating functional intersection of the stress and feeding axes at NPBWR1
doi: 10.1210/en.2003-0536
[2]
noteNPW-23 modulates HPA axis, pain signaling, and cardiovascular tone, consistent with a broad neuromodulatory role in stress-response circuits
[3]
paper
GTG (gold thioglucose) arcuate lesion model used in discovery context, situating NPW in hypothalamic energy-balance circuits that are targets in metabolic disease
doi: 10.1073/pnas.1334189100
openupdated 2026-06-05

Is the very first amino acid of NPW-23 the single most essential contact point that switches on the hunger-regulating receptor?

If one amino acid does most of the work, chemists could build small drug-like molecules that mimic just that contact point. This could lead to oral pills for obesity or eating disorders that are far simpler and cheaper than peptide-based drugs.

The hypothesis
The N-terminal tryptophan of NPW-23 acts as an obligate 'anchor' residue for NPBWR1 engagement, such that its removal or substitution eliminates receptor activation, while the central GRAAGLLMGL segment functions as a conformation-stabilizing spine rather than a primary contact surface.
Why it’s plausible
The peptide name 'W' explicitly references the flanking tryptophans (W1 and W23). In related neuropeptide-GPCR systems, aromatic N-terminal residues frequently insert into the receptor orthosteric pocket and are necessary for activation (e.g., NPY/Y1, orexin/OX1R). Glycine-rich sequences like GRAAG induce backbone flexibility rather than structured helix, suggesting a scaffold role. The high ipTM (0.9382) implies a well-defined predicted complex, within which these functional roles can be structurally assigned.
Why it matters
Identifying W1 as an anchor residue would define the minimal pharmacophore for NPBWR1 agonism, enabling rational design of small-molecule mimetics that reproduce the N-terminal indole contact without the full 23-residue chain.
Plausibility.65
Novelty.50
Impact.65
Basis · grounding1 paper · 3 computed/notes
[1]
sequenceW at position 1 and position 23; GRAAG at positions 14-18 contains two glycines and one alanine, disfavoring rigid secondary structure and suggesting a flexible linker function
[2]
notePeptide named for flanking tryptophan residues, implying structural importance recognized at discovery
[3]
structureHigh pLDDT=84.3 indicates confident per-residue fold; if W1 is buried in the receptor pocket, it would show high local confidence in the complex model
[4]
paper
Reverse-pharmacology discovery via cAMP inhibition assay confirms NPBWR1 functional coupling, providing a defined readout for structure-activity studies
doi: 10.1073/pnas.1334189100
openupdated 2026-06-05

Does the 23-amino-acid version of NPW preferentially switch on the GPR7 receptor while leaving the related GPR8 receptor largely untouched?

If true, NPW-23 could be used to study or treat hunger and stress disorders by activating only one of two closely related receptors, potentially reducing side effects that come from hitting both targets at once. This would matter to anyone developing appetite-suppressing drugs that need to avoid off-target cardiovascular effects.

The hypothesis
NPW-23 binds NPBWR1 (GPR7) with higher intrinsic efficacy than NPBWR2 (GPR8) due to its truncated C-terminus relative to NPW-30, and this differential efficacy is sufficient to produce receptor-subtype-selective physiological outputs in vivo.
Why it’s plausible
NPW-23 and NPW-30 share the same N-terminal sequence but differ at the C-terminus; NPBWR2 is absent in rodents and humans differ in receptor expression patterns. The boltz-2 complex ipTM of 0.9382 indicates a high-confidence predicted interface with NPBWR1, suggesting the N-terminal tryptophan and the central hydrophobic cluster (GRAAGLLMGL) are the dominant contacts. If those contacts saturate NPBWR1 more efficiently than NPBWR2, the shorter peptide would be a functionally selective NPBWR1 agonist rather than a pan-agonist.
Why it matters
Establishing subtype-selective agonism for NPW-23 would reframe it as a pharmacological tool for dissecting NPBWR1-specific circuits (energy balance, HPA axis) from NPBWR2-mediated ones, guiding which receptor to target in metabolic disease.
Plausibility.70
Novelty.45
Impact.60
Basis · grounding1 paper · 3 computed/notes
[1]
structureBoltz-2 complex ipTM=0.9382 with NPBWR1; no comparative prediction against NPBWR2 available, making differential-affinity hypothesis testable
[2]
noteNPW-23 and NPW-30 both produced from prepro-NPW via proteolytic cleavage; C-terminal extension in NPW-30 may engage additional receptor contacts
[3]
paper
Original discovery screen used GPR7 (NPBWR1) and GPR8 (NPBWR2) in parallel, implying both respond to NPW but relative potency/efficacy were not fully resolved
doi: 10.1073/pnas.1334189100
[4]
sequenceC-terminal LLMGL forms a hydrophobic tail; truncation at position 23 vs 30 removes seven residues that could differentially engage NPBWR2 extracellular loops
openupdated 2026-06-05

Does the structurally disordered back half of NPW-23 snap into a rigid, receptor-specific shape upon binding, and does this explain why it does not accidentally activate other brain receptors?

Understanding this shape-shifting behavior could explain why NPW-23 is naturally selective, and could guide design of synthetic peptides or small molecules that inherit that selectivity, reducing the risk of off-target neurological effects in any future drug.

The hypothesis
The GRAAGLLMGL segment of NPW-23 adopts a partial amphipathic conformation upon receptor engagement despite the helix-breaking glycines in isolation, and this induced fit is the structural basis for NPBWR1 subtype selectivity over other neuropeptide GPCRs.
Why it’s plausible
Glycine residues within GRAAG would typically prevent stable helix formation in solution, but receptor-bound peptides frequently adopt helical conformations stabilized by the hydrophobic pocket of transmembrane domains. LLMGL immediately C-terminal to GRAAG is leucine-methionine-glycine-leucine, a hydrophobic sequence capable of forming one face of an amphipathic helix if the GRAAG backbone is appropriately constrained. The high ipTM=0.9382 with NPBWR1 suggests a well-defined bound conformation exists. If this induced amphipathic helix is geometrically complementary only to NPBWR1's transmembrane bundle and not to related GPCRs, it would explain receptor selectivity.
Why it matters
Defining the bound conformation of the C-terminal segment would provide a structural template for peptidomimetic design and explain why NPW does not cross-activate other neuropeptide receptors (e.g., GHSR, MC4R) that share some ligand-space overlap in hypothalamic circuits.
Plausibility.65
Novelty.55
Impact.55
Basis · grounding3 computed/notes
[1]
sequenceGRAAGLLMGL spans positions 14-23; G14, A16, G17 are helix-destabilizing in solution but positions 18-23 (LLMGL) encode hydrophobicity consistent with helix-face packing
[2]
structureBoltz-2 pLDDT=84.3 overall; high per-residue confidence in the complex suggests a defined bound conformation for the C-terminal segment, not a disordered tail
[3]
noteNPW-23 is structurally distinct from Neuropeptide B despite sharing the NPBWR1/2 receptor family, implying sequence-level features drive selectivity
details expand to inspect
full evidence table2 metrics
metricvaluetool
ipTM 0.9381734728813171 boltz-2
ranking score 0.8617234230041504 boltz-2
3-letter notation
Trp-Tyr-Lys-His-Val-Ala-Ser-Pro-Arg-Tyr-His-Thr-Val-Gly-Arg-Ala-Ala-Gly-Leu-Leu-Met-Gly-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). Brain hunger-signaling peptide (Neuropeptide W-23) (pep-04486, v1). PeptideModel. https://peptidemodel.com/card/pep-04486
@peptide{pep04486,
  sequence = {WYKHVASPRYHTVGRAAGLLMGL},
  target   = {npbwr1},
  author   = {peptidemodel},
  year     = {2026},
  status   = {bioassayed}
}
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 3 papers
[1] primary
[3]
A Role for Neuropeptide W in the Regulation of Feeding Behavior
Mondal MS, Yamaguchi H, Date Y, Shimbara T Endocrinology 2003
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