pe
pep-10715 v1 CC-BY-SA-4.0

Neuropeptide Y: brain chemical that drives hunger and stress responses

A natural signaling peptide found throughout the brain and nervous system that stimulates appetite, regulates stress, and controls blood vessel tone; this is the sheep version, used as a lab research tool.

statussynthesized targetNPBWR1 length36 aa refs8
snapshot sparse 10% confidence
Class
Endogenous neuropeptide — ovine (sheep) form
Status
No approved therapeutic status identified in attached sources
Main caveat
Source file provides the ovine amino-acid sequence and a single 1989 structural characterization reference only. No efficacy, safety, mechanism, or clinical data are attached to this card.
status 4 / 5
prediction metrics boltz-2 2.2.1
ipTM0.888
pTM0.883
avg pLDDT84.8
ranking score0.856
STRUCTURE · PEP-10715 × 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
YPSKPDNPGDDAPAEDLA RYYSALRHYINLITRQRY
overview readme

What this is

Neuropeptide Y (NPY) is a 36-amino acid signaling peptide that is one of the most abundant neuropeptides in the mammalian brain and peripheral nervous system. Found in virtually all vertebrates, it acts as a chemical messenger that regulates hunger, stress responses, sleep, and blood vessel tone. The sequence stored here is the sheep (Ovis aries) form of NPY; sheep NPY differs from human and rat NPY at position 10 (Asp instead of Glu) and shares Leu at position 17 with pig and bovine NPY, making it one of three distinct mammalian structural variants (Sillard and colleagues, 1989).

History

NPY was first isolated and characterized in the early 1980s as part of a broader effort to describe the neuropeptide Y peptide family, which also includes peptide YY (PYY) and pancreatic polypeptide (PP). The sheep-specific sequence was characterized by Sillard and colleagues (1989, FEBS Letters), who found it differed from the six previously described mammalian forms at position 10, establishing three structural classes of mammalian NPY. Interest in NPY's receptor system expanded substantially after the deorphanization of GPR7 and GPR8 as the receptors for the related neuropeptides B (NPB) and W (NPW) — receptors now designated NPBWR1 and NPBWR2 (Singh and colleagues, 2006, British Journal of Pharmacology).

What it does

NPY acts as a potent orexigenic (appetite-stimulating) signal in the hypothalamus, promoting food intake and contributing to energy balance regulation. It also functions as an endogenous "anti-stress" peptide: central NPY signaling is recruited in response to stressors to help restore homeostasis, suppressing the HPA axis and inhibiting the release of stress hormones ACTH and cortisol. Beyond hunger and stress, NPY participates in regulating sleep and in sympathetic control of blood vessel tone — NPY released from sympathetic nerves contributes to vasoconstriction in the skin. NPY has five recognized receptor subtypes across the central and peripheral nervous system (Y1R–Y5R).

Evidence

  • Human: NPY is an endogenous peptide well-established in human physiology. Genetic variation in the NPBWR1 receptor — the receptor family this card links NPY to — has been associated with individual differences in social cognition; a single nucleotide polymorphism of NPBWR1 influenced evaluation of facial expressions in a human study (Watanabe and colleagues, 2012, PLoS ONE). No human clinical trials using exogenous NPY as a therapeutic have been identified in the dossier.
  • Animal: Animal studies have established NPY as a key hypothalamic regulator of food intake and stress responses. NPY's roles in circadian regulation, sleep promotion, and HPA axis suppression are supported by rodent and other vertebrate models.
  • In vitro: Structural-activity relationship (SAR) work on non-peptidic NPBWR1 (GPR7) antagonists has characterized receptor binding properties at the NPBWR1 target (Guerrero and colleagues, 2013, Bioorganic & Medicinal Chemistry Letters).

Known effects

  • Appetite stimulation (orexigenic) — Well-established in animal models; central NPY signaling promotes food intake.
  • HPA axis suppression / anti-stress — Preclinical models; NPY inhibits ACTH and cortisol release.
  • Sleep promotion — NPY promotes sleep in animal models.
  • Sympathetic vasoconstriction — NPY participates in reflex cutaneous vasoconstriction; established across animal and human studies.
  • Social cognition modulation — NPBWR1 SNP association with facial expression evaluation in humans (Watanabe and colleagues, 2012).

Mechanism

NPY's classical actions are mediated through five G protein-coupled receptor subtypes — Y1R, Y2R, Y3R, Y4R, and Y5R — distributed throughout the central and peripheral nervous system. This card's platform target assignment is NPBWR1 (GPR7), a class A GPCR originally deorphanized as the receptor for the structurally related neuropeptides B and W (NPB/NPW). NPB and NPW were identified as the cognate endogenous ligands for GPR7/NPBWR1; NPW mRNA is highly expressed in the substantia nigra and at moderate levels in the amygdala and hippocampus in humans (Singh and colleagues, 2006). The NPBWR1 system modulates energy homeostasis, inflammatory pain, and emotional processing (Sakurai, 2013, Frontiers in Endocrinology). A second receptor, NPBWR2 (GPR8), is present in humans but absent in rodents (Wojciechowicz and colleagues, 2021, International Journal of Molecular Sciences). The Chottova Dvorakova (2018, Frontiers in Physiology) review maps the full distribution and functional scope of the NPB/W signaling network.

Safety signals

NPY is an endogenous peptide present throughout the nervous system in all mammalian species examined. No adverse safety signals from exogenous administration are documented in the dossier sources. The opioid receptor evolution context provided by Dreborg and colleagues (2008, PNAS) situates the NPBWR1 receptor within a broader GPCR family context; no safety-relevant off-target interactions at opioid receptors are characterized for NPY specifically in the dossier.

Related peptides

The NPY family includes structurally related peptides that share the PP-fold motif and act at overlapping receptor sets:

  • Peptide YY (PYY) — a 36-amino acid gut hormone co-expressed with GLP-1 in intestinal L-cells; anorexigenic counterpart to NPY's orexigenic action.
  • Neuropeptide B (NPB) — primary endogenous ligand for NPBWR1 (GPR7), the platform target assigned to this card (Singh and colleagues, 2006).
  • Neuropeptide W (NPW) — co-ligand at NPBWR1 and NPBWR2 alongside NPB (Singh and colleagues, 2006).
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 2026-06-05

Could the tiny difference between sheep and human NPY change how strongly it sticks to the NPBWR1 receptor?

If true, drug developers would know that animal model choice matters for NPY-related drugs, and they could design peptides that selectively favor human or sheep-like binding for better therapeutic control.

The hypothesis
Sheep NPY (D10) binds NPBWR1 with measurably different kinetics than human NPY (E10) due to the altered electrostatic surface at the N-terminal turn.
Why it’s plausible
The D10 substitution introduces a negative charge where human/rat NPY has a glutamate, altering local electrostatics in a region known to influence receptor engagement across the NPY family. The high ipTM (0.89) for the NPY-NPBWR1 complex suggests genuine interaction potential, but the single-residue difference between mammalian variants has not been functionally tested for NPBWR1.
Why it matters
If true, it would reveal that even highly conserved neuropeptides have species-specific pharmacology at deorphanized receptors, with implications for choosing animal models in NPBWR1 drug development and for interpreting cross-species NPY data.
Plausibility.55
Novelty.70
Impact.45
Basis · grounding1 paper · 2 computed/notes
[1]
sequenceSheep NPY has Asp at position 10; human and rat NPY have Glu at position 10. The D10 vs E10 difference changes side-chain length and local electrostatics in the N-terminal region.
[2]
structureboltz-2/complex ipTM=0.888, pLDDT=84.8 for NPY-NPBWR1 complex suggests a credible binding pose but does not resolve whether D10 or E10 is preferred at the interface.
[3]
paper
Sillard et al. (1989) established that sheep NPY differs from other mammalian forms at position 10, defining three structural classes of mammalian NPY.
doi: 10.1016/0014-5793(89)81669-2
openupdated 2026-06-05

Could the same peptide that makes us hungry also prevent the adrenal gland from pumping out too much adrenaline?

If true, doctors could explore NPY-like drugs for high blood pressure or panic disorders by targeting the adrenal gland, using a well-known peptide in an entirely new way.

The hypothesis
NPY, traditionally viewed as an orexigenic brain peptide, is endogenously co-released with catecholamines in the adrenal medulla and functions as a local paracrine brake on excessive catecholamine secretion via NPBWR1.
Why it’s plausible
NPY is known to coexist with catecholamines in sympathetic nerves and adrenal chromaffin cells. NPBWR1 is expressed in adrenal medulla. If NPY activates NPBWR1 locally, it could initiate an inhibitory feedback loop, repurposing NPY from a hunger signal to a peripheral stress modulator.
Why it matters
If true, NPY would have a dual, opposing role: central appetite stimulation and peripheral catecholamine restraint. This would explain why global NPY knockout or overexpression produces complex phenotypes and would suggest adrenal-specific NPY mimetics for hypertension or anxiety.
Plausibility.50
Novelty.55
Impact.60
Basis · grounding2 papers · 1 computed/note
[1]
paper
Npbwr1 mRNA is expressed in adrenal medulla as well as cortex, placing the receptor in the catecholamine-secreting compartment.
doi: 10.3389/fendo.2013.00023
[2]
noteNPY is one of the most abundant neuropeptides in the peripheral nervous system and regulates blood vessel tone, suggesting widespread peripheral signaling beyond the brain.
[3]
paper
Transient expression studies of neuropeptide W suggest dynamic regulation of NPBWR1 ligands in stress-related tissues, supporting the concept of ligand competition in adrenal signaling.
doi: 10.3389/fphys.2018.00981
openupdated 2026-06-05

Could a single shorter side chain at position 10 change the bend angle of NPY and alter how its back half meets the receptor?

If true, scientists could redesign NPY-like drugs by tweaking hinge residues far from the binding surface, creating new variants with better receptor fit and fewer side effects.

The hypothesis
The proline-rich N-terminal segment YPSKPDNPGD (residues 1-10) of sheep NPY acts as a conformational switch: D10 stabilizes a tighter turn than E10, altering the presentation of the downstream alpha-helical hairpin to NPBWR1.
Why it’s plausible
NPY adopts a characteristic PP-fold with an N-terminal polyproline helix and a C-terminal alpha-helical hairpin. Position 10 sits at the junction between these elements. Asp versus Glu at this pivot could change turn geometry due to side-chain length and hydrogen-bonding differences, propagating to the receptor-facing C-terminal region.
Why it matters
If true, it would mean that single-residue variation at a fold junction can allosterically control receptor engagement without touching the binding epitope directly, opening a design principle for NPY-family peptide engineering.
Plausibility.40
Novelty.60
Impact.50
Basis · grounding1 paper · 2 computed/notes
[1]
sequenceSheep NPY residues 1-10: YPSKPDNPGD; human NPY: YPSKPDNPGED (E10). The D10 deletion removes one methylene group from the side chain at the proline-rich to helical transition.
[2]
structureOverall complex confidence is high (ipTM=0.888, pLDDT=84.8) but structure predictions do not resolve whether D10 or E10 produces a different turn angle or hairpin presentation.
[3]
paper
Sillard et al. (1989) defined three mammalian NPY structural classes based on position 10 and 17 substitutions, implying these residues are under selective pressure.
doi: 10.1016/0014-5793(89)81669-2
details expand to inspect
full evidence table2 metrics
metricvaluetool
ipTM 0.8876509666442871 boltz-2
ranking score 0.8559975028038025 boltz-2
3-letter notation
Tyr-Pro-Ser-Lys-Pro-Asp-Asn-Pro-Gly-Asp-Asp-Ala-Pro-Ala-Glu-Asp-Leu-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: brain chemical that drives hunger and stress responses (pep-10715, v1). PeptideModel. https://peptidemodel.com/card/pep-10715
@peptide{pep10715,
  sequence = {YPSKPDNPGDDAPAEDLARYYSALRHYINLITRQRY},
  target   = {npbwr1},
  author   = {peptidemodel},
  year     = {2026},
  status   = {synthesized}
}
related peptides 3 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 8 papers
[1]
Sheep neuropeptide Y
Sillard, R. et al. FEBS Letters 1989
evidence
[2] supporting
[4]
SAR analysis of novel non-peptidic NPBWR1 (GPR7) antagonists
Guerrero, M. et al. Bioorganic & Medicinal Chemistry Letters 2013
supporting
[6] supporting
[7]
Evolution of vertebrate opioid receptors
Dreborg, S. et al. Proceedings of the National Academy of Sciences 2008
supporting
discussion no comments
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