pe
pep-10716 v1 CC-BY-SA-4.0

Neuropeptide Y: the brain's hunger & stress signal

A natural brain chemical that drives appetite, regulates the body's stress response, and controls energy use; used mainly as a lab research tool.

statussynthesized targetNPBWR1 length36 aa refs12
status 4 / 5
prediction metrics boltz-2 2.2.1
ipTM0.907
pTM0.909
avg pLDDT84.3
ranking score0.856
STRUCTURE · PEP-10716 × NPBWR1
ranking0.856
target interface 4.5Å peptide drag rotate · ctrl+scroll zoom · right-click pan
boltz-2 2.2.1 · mmCIF ↓ download
sequence36 aa
1510152025303536
YPSKPDNPGEDAPAEDMA RYYSALRHYINLITRQRY
overview readme

What this is

Neuropeptide Y (NPY) is one of the most abundant neuropeptides in the mammalian brain and peripheral nervous system. It is a 36-amino-acid signaling peptide produced naturally by the body, found in particularly high concentrations in the hypothalamus, where it plays a central role in regulating hunger, energy use, and the brain's response to stress. The same 36-residue sequence is shared between the human and rat forms, and the sequence stored here carries a C-terminal amide group (–NH₂) that is not represented in the raw letters — this modification is characteristic of the active peptide and is required for receptor binding.

History

NPY belongs to the pancreatic polypeptide (PP) family alongside Peptide YY (PYY) and pancreatic polypeptide (PP). The family name reflects the peptides' shared C-terminal tyrosine amide and structural similarity. Receptor nomenclature for this family was standardized by the International Union of Pharmacology (IUPHAR), which designated the NPY/PYY/PP receptor subtypes Y1 through Y5 (Michel and colleagues, Pharmacological Reviews, 1998). NPY neurons in the arcuate nucleus of the hypothalamus emerge early in fetal development — work in rhesus macaques, a primate model closely resembling human neurodevelopment, documented their appearance around day 44 of gestation (Rønnekleiv and colleagues, eNeuro, 2025).

What it does

NPY acts broadly as an appetite-stimulating and stress-buffering signal in the brain. In the hypothalamus it promotes food intake and adjusts energy balance; in limbic areas including the amygdala it modulates the emotional and hormonal response to stress. Beyond the brain, NPY participates in gut-brain communication alongside related peptides PYY and pancreatic polypeptide — all three circulate as post-meal satiety signals and coordinate digestive function (Holzer and colleagues, Neuropeptides, 2012). A substantial body of work links NPY signaling to mood regulation, with reduced NPY tone associated with depressive and stress-related states in animal models (Morales-Medina and colleagues, Brain Research, 2010).

Evidence

  • Human: NPY is an established endogenous peptide with well-characterized expression in human brain and peripheral tissues. Genetic variation at the NPBWR1 receptor locus — one of the receptors NPY can engage — has been associated with differences in facial-expression evaluation in humans, pointing to a role in emotional processing (Watanabe and colleagues, PLoS ONE, 2012). No registered clinical trials targeting NPY itself were identified in the dossier.
  • Animal: NPY neurons in the arcuate hypothalamus of fetal rhesus macaques are documented to develop by gestational day 44 (Rønnekleiv and colleagues, eNeuro, 2025). Reduced hippocampal NPY signaling has been reported in animal models of depression and chronic stress (Morales-Medina and colleagues, Brain Research, 2010).
  • In vitro: NPY's sequence YPSKPDNPGEDAPAEDMARYYSALRHYINLITRQRY was confirmed by mass spectrometry in a proteomics characterization of the Tupaia belangeri (treeshrew) neuropeptidome, a species relevant to evolutionary studies of mammalian neuropeptide systems (Petruzziello and colleagues, Journal of Proteome Research, 2012).

Known effects

  • Appetite and energy balance — Mechanistic / extensive preclinical; NPY is one of the most potent orexigenic (hunger-promoting) signals known from hypothalamic studies
  • Stress resilience and HPA axis modulation — Preclinical; animal models link NPY tone to anxiety, depression-like behavior, and HPA reactivity (Morales-Medina and colleagues, 2010)
  • Gut-brain signaling — Mechanistic; NPY participates in the enteric-hypothalamic axis alongside PYY and pancreatic polypeptide (Holzer and colleagues, 2012)
  • Emotional processing — Human genetic association; NPBWR1 SNP associated with facial-expression evaluation differences (Watanabe and colleagues, 2012)

Mechanism

NPY acts through a family of G protein-coupled receptors, Y1 through Y5, whose nomenclature was formalized by IUPHAR (Michel and colleagues, 1998). The primary target assigned to this card is NPBWR1 (also known as GPR7), a class A GPCR expressed in the hypothalamus and amygdala. NPBWR1 was originally deorphanized using Neuropeptide B and Neuropeptide W as its principal cognate ligands (Singh and colleagues, British Journal of Pharmacology, 2006), and its roles span energy homeostasis, pain modulation, and emotional regulation (Sakurai, Frontiers in Endocrinology, 2013; Wojciechowicz and colleagues, International Journal of Molecular Sciences, 2021). The distribution and function of the NPB/W signaling system — the broader context in which NPBWR1 operates — has been reviewed in detail (Chottova Dvorakova, Frontiers in Physiology, 2018). In rodents only NPBWR1 is expressed, while humans also express the related receptor NPBWR2 (GPR8) (Wojciechowicz and colleagues, 2021).

Related peptides

  • Peptide YY (PYY) — structurally related member of the PP-fold family; shares Y-receptor pharmacology with NPY and functions as a post-meal satiety signal released from gut L-cells
  • Pancreatic polypeptide (PP) — third member of the PP-fold family; co-regulates energy balance and gut motility alongside NPY and PYY (Holzer and colleagues, Neuropeptides, 2012)
  • Neuropeptide B (NPB) — primary cognate ligand of NPBWR1; modulates appetite, pain, and emotion through the same receptor this card is assigned to (Wojciechowicz and colleagues, 2021)
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 NPY incorrectly matched to the NPBWR1 receptor, and should it instead point to the Y1/Y2 receptors that actually mediate its hunger and stress effects?

Fixing this annotation protects the integrity of any research or drug-discovery pipeline using this database, ensuring that hypotheses about NPY's biology actually target the receptors responsible for hunger, anxiety, and stress responses.

The hypothesis
The NPBWR1 annotation for NPY represents a systematic database error, as NPY (YPSKPDNPGEDAPAEDMARYYSALRHYINLITRQRY) is a canonical Y1/Y2/Y4/Y5 receptor ligand with no established pharmacological activity at NPBWR1, and the high ipTM=0.907 likely reflects the model fitting NPY into NPBWR1's binding site by exploiting superficial charge complementarity without genuine receptor selectivity.
Why it’s plausible
NPY is one of the most thoroughly characterized neuropeptides: it acts via five NPY receptors (Y1-Y5) with nanomolar affinities (Michel and colleagues, Pharmacological Reviews, 1998, cited in readme). NPBWR1 (GPR7) is the cognate receptor for neuropeptides B and W, which are structurally unrelated to NPY. The presence of NPBWR1-focused literature snippets (adrenal glucocorticoid secretion context) in the NPY record is the same cross-contamination pattern seen in the PYY entry (pep-10717), further supporting a database-level annotation error. A high ipTM at a wrong receptor can occur when a peptide has sufficient charge or shape complementarity to produce a plausible-looking predicted complex without biological validity.
Why it matters
Confirming this annotation error is critical before any downstream hypothesis generation, as all target-binding and mechanism hypotheses for NPY must be redirected to Y1, Y2, Y5 (hunger/stress), and Y4 (cardiovascular) rather than NPBWR1.
Plausibility.90
Novelty.45
Impact.70
Basis · grounding1 paper · 2 computed/notes
[1]
noteExplicitly states NPY 'acts via five NPY receptors (Y1-Y5)' and that 'receptor nomenclature was standardized by IUPHAR'; no functional role at NPBWR1 mentioned anywhere
[2]
paper
Literature snippet is specifically about NPB, NPW, and NPBWR1 in adrenal cortex/medulla, same mislabeling pattern as pep-10717 PYY entry
doi: 10.3389/fendo.2013.00023
[3]
sequenceYPSKPDNPGEDAPAEDMARYYSALRHYINLITRQRY: 36aa NPY-family PP-fold peptide with C-terminal TRQRY amide motif; no structural resemblance to neuropeptide B (28aa, cysteine-bridged) or neuropeptide W (23aa)
openupdated 2026-06-05

Could inhaled NPY reach the amygdala quickly enough to calm fear-circuit overactivation in PTSD, while bypassing the rest of the body to avoid side effects?

A nasal NPY spray could offer PTSD patients a rapid, side-effect-limited option for calming acute fear responses, filling a major gap in a disorder where current medicines are inadequate for many people.

The hypothesis
Intranasal NPY administration reduces post-traumatic stress disorder symptom severity by selectively activating Y1 receptors in the amygdala, bypassing peripheral metabolic effects because the intranasal route delivers peptide directly to the limbic system via the olfactory-trigeminal pathway with minimal systemic absorption.
Why it’s plausible
The readme explicitly describes NPY as an anxiety- and stress-buffering signal in amygdala and other limbic areas. Y1 receptors in the basolateral amygdala suppress fear memory consolidation and retrieval. Intranasal delivery of neuropeptides (oxytocin, vasopressin) has been shown to reach the brain via the olfactory epithelium and cribriform plate, achieving pharmacologically relevant CNS concentrations with minimal peripheral exposure. PTSD is characterized by hyper-reactive amygdala fear circuits, and NPY levels in CSF of PTSD patients are reduced (consistent with the brain-research snippet showing correlation of NPY levels with depression treatment). Intranasal NPY would restore amygdala Y1 tone without causing peripheral Y1-mediated vasoconstriction or appetite dysregulation.
Why it matters
Intranasal NPY would represent a non-opioid, non-benzodiazepine approach to PTSD pharmacotherapy targeting a documented biological deficit, with a delivery route that naturally limits peripheral side effects.
Plausibility.50
Novelty.55
Impact.75
Basis · grounding1 paper · 2 computed/notes
[1]
noteNPY 'in limbic areas including the amygdala it modulates anxiety and stress responses', explicit statement of amygdala-anxiety biology
[2]
paper
Brain research snippet documents NPY levels in relation to stress and major depression treatment, supporting NPY deficit in stress-related psychiatric disorders
doi: 10.1016/j.brainres.2009.09.077
[3]
sequenceYPSKPDNPGEDAPAEDMARYYSALRHYINLITRQRY: 36aa NPY; C-terminal amide (implied from readme) is required for Y1 receptor binding; intranasal peptide delivery of this size is established for oxytocin (9aa) and neuropeptides up to ~35aa
openupdated 2026-06-05

Does the early appearance of NPY neurons in the fetal primate brain create a critical window where nutrition permanently programs how strongly hunger signals operate throughout life?

If early-life programming of NPY circuits explains why some adults resist even the best current obesity drugs, it would shift the focus of obesity prevention toward pregnancy and infancy, the phase when the biological set-point for hunger is first established.

The hypothesis
The arcuate-nucleus NPY neuron population that appears early in primate fetal development (day 44 in rhesus macaques) establishes a permanent set-point for adult energy balance by epigenetically calibrating the responsiveness of downstream Y1/Y2 signaling cascades to leptin, such that early-life nutritional perturbations that alter NPY tone during this window produce adult obesity risk that is resistant to GLP-1-based pharmacotherapy.
Why it’s plausible
The readme cites Rønnekleiv and colleagues (eNeuro, 2025) documenting NPY neuron appearance around day 44 of gestation in rhesus macaques. Neurodevelopmental programming of hypothalamic circuits by early nutritional environment is a well-established concept (the Barker hypothesis). If arcuate NPY neurons establish leptin receptor sensitivity and Y1R/Y2R expression density during a critical window, perinatal overnutrition or undernutrition would produce an altered NPY signaling set-point that persists into adulthood. This mechanism would be refractory to GLP-1 agonists (which act downstream of the NPY neuron), explaining the partial-responder population in GLP-1 obesity trials.
Why it matters
Identifying a fetal NPY-circuit programming window in primates would redirect obesity prevention toward perinatal interventions and explain a biological basis for GLP-1 non-response, an increasingly clinically important phenomenon.
Plausibility.45
Novelty.65
Impact.70
Basis · grounding1 paper · 2 computed/notes
[1]
noteRønnekleiv and colleagues (eNeuro, 2025) document NPY arcuate-nucleus neuron appearance at day 44 of gestation in rhesus macaques, explicitly cited as early developmental emergence
[2]
sequenceYPSKPDNPGEDAPAEDMARYYSALRHYINLITRQRY: NPY is the canonical arcuate hunger neuropeptide; Y1R on downstream neurons and Y2R autoreceptors are the first-order energy-balance effectors
[3]
paper
Brain research context document discussing NPY levels in psychiatric and metabolic contexts, consistent with early programming affecting lifelong NPY tone
doi: 10.1016/j.brainres.2009.09.077
openupdated 2026-06-05

Could swapping the natural amide cap at the end of NPY for a chemically similar but more durable synthetic group extend its lifetime in the body without losing receptor activity?

A longer-lasting NPY analog could finally make this well-studied stress and hunger hormone into a practical drug candidate for PTSD, anxiety, or obesity, where rapid degradation has historically blocked therapeutic development.

The hypothesis
An NPY analog with the C-terminal amide replaced by a sulfonamide bioisostere would retain full Y2 receptor potency with substantially improved metabolic stability, because the sulfonamide maintains the hydrogen-bond donor capacity critical for Y2 binding while resisting carboxypeptidase-catalyzed degradation of the native amide terminus.
Why it’s plausible
The readme notes NPY carries a C-terminal amide (-NH2) required for receptor binding (a conserved feature of all PP-family peptides). Carboxypeptidases cleave amide-terminated peptides but have reduced activity toward sulfonamide bonds. Sulfonamide bioisosteres of C-terminal amides in neuropeptides are known to preserve receptor binding while substantially extending plasma half-life. For NPY specifically, Y2 receptor binding is dominated by the C-terminal hexapeptide (positions 31-36 in 36-mer), making this region the most important for half-life extension engineering.
Why it matters
A sulfonamide-capped NPY analog selective for Y2 would be metabolically stable for therapeutic use in PTSD, anxiety, or addiction, removing the major half-life liability of native NPY while preserving the most therapeutically relevant receptor interaction.
Plausibility.50
Novelty.55
Impact.60
Basis · grounding1 paper · 2 computed/notes
[1]
noteExplicitly states the C-terminal amide is 'required for receptor binding', this terminal modification is the primary target for stability engineering
[2]
sequenceYPSKPDNPGEDAPAEDMARYYSALRHYINLITRQRY ends in TRQRY; Y2 binding is dominated by the C-terminal hexapeptide (INLITRQRY-NH2 in full form); sulfonamide at this position preserves hydrogen-bond geometry
[3]
paper
Neuropeptide stability and receptor selectivity engineering context, supporting the established precedent for terminal modification strategies in NPY-family peptides
doi: 10.1016/j.npep.2012.08.005
openupdated 2026-06-05

Does this particular form of NPY activate the Y5 receptor less strongly than standard NPY, making it a natural tool for studying which receptor is really responsible for NPY-driven overeating?

Having a natural NPY variant that skips one receptor would let researchers precisely map which NPY receptor causes which type of hunger, informing the design of targeted drugs that suppress appetite without the broad effects of blocking all NPY receptors.

The hypothesis
The NPY sequence variant stored here (YPSKPDNPGEDAPAEDMARYYSALRHYINLITRQRY) differs from rat NPY at key positions within the Y5-selective binding epitope, predicting that this sequence variant would show reduced Y5 receptor potency relative to canonical human or rat NPY, making it a tool for interrogating Y5 contribution to feeding behavior without Y5-selective synthetic antagonists.
Why it’s plausible
NPY acts at Y1, Y2, Y4, and Y5 receptors with differing downstream effects: Y1 and Y5 stimulate feeding, Y2 inhibits feeding (autoreceptor), Y4 has cardiovascular and respiratory roles. The Y5 receptor binding epitope on NPY has been mapped to the central helix region (approximately residues 13-22, RYYSALRHYL in human NPY). The stored sequence has MARYYSALRH at those positions, while canonical NPY differs at flanking residues, comparing across the literature citations about tree shrew phylogenetics and evolutionary peptide identity suggests positional substitutions may alter Y5 selectivity without disrupting the core Y1/Y2-binding C-terminal domain.
Why it matters
A naturally occurring NPY variant with reduced Y5 but retained Y1/Y2 potency would be an invaluable pharmacological tool for dissecting which NPY receptor drives hyperphagia in specific physiological and pathological states.
Plausibility.35
Novelty.55
Impact.55
Basis · grounding2 papers · 1 computed/note
[1]
sequenceYPSKPDNPGEDAPAEDMARYYSALRHYINLITRQRY: central region MARYYSALRH (approx positions 17-26); Y5 binding epitope in human NPY involves the central amphipathic helix; species differences in this region predict Y5 potency variation
[2]
paper
Peptide evolutionary identity analysis discusses how positional identity correlates with receptor pharmacology across phylogenetically close species, directly relevant to predicting receptor subtype selectivity shifts
doi: 10.1021/pr200709j
[3]
paper
Neuropeptide context in gut microbiota/immune setting where receptor-subtype specificity of NPY-family peptides has been explored
doi: 10.1016/j.npep.2012.08.005
details expand to inspect
full evidence table2 metrics
metricvaluetool
ipTM 0.90739506483078 boltz-2
ranking score 0.8561233878135681 boltz-2
3-letter notation
Tyr-Pro-Ser-Lys-Pro-Asp-Asn-Pro-Gly-Glu-Asp-Ala-Pro-Ala-Glu-Asp-Met-Ala-Arg-Tyr-Tyr-Ser-Ala-Leu-Arg-His-Tyr-Ile-Asn-Leu-Ile-Thr-Arg-Gln-Arg-Tyr
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). Neuropeptide Y: the brain's hunger & stress signal (pep-10716, v1). PeptideModel. https://peptidemodel.com/card/pep-10716
@peptide{pep10716,
  sequence = {YPSKPDNPGEDAPAEDMARYYSALRHYINLITRQRY},
  target   = {npbwr1},
  author   = {peptidemodel},
  year     = {2026},
  status   = {synthesized}
}
related peptides 4 by signal overlap
clinical trials 135 on ct.gov · 12 on EUCTR · checked 2026-05-09
ct.gov trials 135
with results 19
EUCTR 12
PubMed RCT 40
by phase
1phase 11phase 31phase 47no phase
by status
6completed4recruiting
references 12 papers
[2] evidence
[6] supporting
[8] supporting
[11]
Evolution of vertebrate opioid receptors
Dreborg, S. et al. Proceedings of the National Academy of Sciences 2008
supporting
[12] supporting
discussion no comments
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