pe
pep-10717 v1 CC-BY-SA-4.0

Peptide YY: gut hormone that tells the brain you're full

A natural hormone released by the intestine after eating that signals fullness to the brain and reduces food intake; studied as a potential obesity treatment but not yet an approved drug.

statussynthesized targetNPBWR1 length36 aa refs8
snapshot sequence_only 15% confidence
Class
Gut peptide / neuropeptide (species-specific form)
Status
Research and catalog entry; no approved therapeutic status identified
Best-supported effect
Sequence characterized from rabbit (Oryctolagus cuniculus) gastrointestinal tissue; no bioactivity or therapeutic effect supported by this card's source file
Main caveat
Compiled source provides sequence identity and species origin only; no biological assay, animal experiment, or human data attached to this card's source file
status 4 / 5
prediction metrics boltz-2 1.0
ipTM0.878
pTM0.877
avg pLDDT83.5
ranking score0.843
STRUCTURE · PEP-10717 × NPBWR1
ranking0.843
target interface 4.5Å peptide drag rotate · ctrl+scroll zoom · right-click pan
boltz-2 1.0 · mmCIF ↓ download
sequence36 aa
1510152025303536
YPSKPEAPGEDASPEELN RYYASLRHYLNLVTRQRY
overview readme

What this is

Peptide YY (PYY) is a gut hormone released by specialised intestinal cells called L cells after a meal. It belongs to the neuropeptide Y family alongside neuropeptide Y (NPY) and pancreatic polypeptide, and the amount secreted is roughly proportional to the caloric content of food consumed (Karra and colleagues, 2009). PYY circulates in two principal forms: the full-length PYY(1-36), which binds a broad range of NPY-family receptors, and the truncated PYY(3-36), which is generated when an enzyme called DPP-IV clips off the first two residues and selectively activates the Y2 receptor to reduce food intake. No drug based on PYY has reached regulatory approval; the peptide currently has no approved clinical use.

The 36-residue sequence stored here (YPSKPEAPGEDASPEELNRYYASLRHYLNLVTRQRY) may represent a non-human species variant: position 3 reads Ser in this entry, whereas human PYY carries Ile at that position.

History

PYY was first described in tissues of the human gut in the mid-1980s; Adrian and colleagues (1985) documented its distribution and postprandial release, establishing it as a genuine circulating gut hormone. Interest intensified with the observation that PYY is co-localised with glucagon-like peptide-1 (GLP-1) in the L cells of the gastrointestinal mucosa (Karra and colleagues, 2009). Grandt and colleagues (1994) characterised both PYY(1-36) and PYY(3-36) and showed they differ in receptor selectivity, laying the groundwork for understanding the distinct biology of each form. The discovery that PYY(3-36) reduced feeding in both rodents and humans made it a focus of obesity research in the early 2000s; a subsequent clinical study by Gantz and colleagues (2007) explored intranasal delivery as a weight-loss strategy in obese adults.

What it does

After a meal, L cells in the distal small intestine and colon release PYY into the bloodstream in proportion to the calories consumed (Karra and colleagues, 2009). This signal travels to the brain — particularly the hypothalamus and brainstem — and signals satiety, reducing the urge to keep eating. PYY also slows gastric emptying and suppresses pancreatic and gastric secretion, actions sometimes called the "colonic brake" (Nightingale and colleagues, 1996, cited in Karra and colleagues, 2009).

The truncated form PYY(3-36) is the more potent appetite suppressor: it preferentially activates the Y2 receptor and, in doing so, inhibits both appetite-promoting (NPY) and appetite-suppressing (POMC) hypothalamic neurons, ultimately reducing food intake (Karra and colleagues, 2009). Although PYY(1-36) has a circulating half-life of approximately 10 minutes in humans, postprandial plasma levels remain elevated for up to 6 hours because of sustained L-cell release (Frontiers in Nutrition, 2015).

PYY levels are markedly elevated after Roux-en-Y gastric bypass surgery; this rise is thought to contribute to the appetite suppression and long-term weight loss that follow the procedure (Chan and colleagues, 2006, cited in Karra and colleagues, 2009).

Evidence

  • Human: Gantz and colleagues (2007) conducted a clinical study of intranasal PYY(3-36) for weight reduction in obese adults, published in the Journal of Clinical Endocrinology and Metabolism; this remains one of the few published interventional studies of exogenous PYY administration in humans. A subsequent randomised study combined PYY with GLP-1 and oxyntomodulin and reported improvements in body weight and glycaemia in obese adults with prediabetes or type 2 diabetes (Frontiers in Endocrinology, 2021).
  • Animal: Genetic ablation of PYY in mice produced hyperinsulinaemia and obesity, demonstrating that endogenous PYY is required for normal metabolic homeostasis (Boey and colleagues, 2006, cited in Karra and colleagues, 2009). Intermittent intravenous infusion of PYY(3-36) reduced daily food intake in rodent models.
  • In vitro / mechanistic: PYY(3-36) inhibits both POMC and NPY neurons in hypothalamic preparations, demonstrating central action on the energy-balance circuitry (Karra and colleagues, 2009).

Known effects

  • Appetite suppression (postprandial satiety signal) — Established physiological role; human and animal data (Karra and colleagues, 2009)
  • Slowing of gastric emptying / colonic brake — Physiological; documented in human gut hormone studies
  • Elevated after bariatric surgery — Observed in human cohorts; putative contributor to post-surgical satiety
  • Obesity when genetically absent — Preclinical (mouse knockout model)

Safety signals

The main adverse effect observed in early human administration studies was nausea. Gantz and colleagues (2007) reported nausea as a limiting factor in the intranasal PYY(3-36) trial, a finding that has tempered enthusiasm for exogenous PYY as a standalone therapeutic. The physiological form circulates in plasma after every meal without ill effect; adverse signals are associated with pharmacological delivery at supraphysiological levels.

Regulatory status

  • US: No FDA-approved drug. Not a scheduled substance. No compounding designation.
  • EU: No EMA-approved product.
  • WADA: No current prohibition specifically targeting PYY; its physiological nature means it is not on the prohibited list as of available records.

Mechanism

PYY(3-36) exerts its anorexigenic effect primarily through the Y2 receptor (Y2R), a Gi-coupled GPCR expressed on NPY-releasing neurons in the arcuate nucleus of the hypothalamus, on vagal afferents in the nodose ganglion, and in brainstem nuclei (Karra and colleagues, 2009). Y2R is a presynaptic autoreceptor on NPY neurons; its activation reduces NPY release and simultaneously permits POMC/CART neurons to increase their output, shifting the hypothalamic balance toward satiety. Full-length PYY(1-36) activates Y1R, Y2R, Y4R, and Y5R with less selectivity, producing a broader — and partially orexigenic, via Y1/Y5 — pharmacological profile.

The stored sequence (YPSKPEAPGEDASPEELNRYYASLRHYLNLVTRQRY) is the unmodified linear sequence; no fatty-acid conjugation, acetyl cap, or amide terminus is present. The C-terminal -QRY motif, conserved across the NPY family, is essential for receptor recognition.

The card's primary assigned target is NPBWR1 (GPR7, the neuropeptide B/W receptor 1). NPBWR1 is structurally related to the NPY receptor family and shares some ligand-binding space (Sakurai, 2013; Wojciechowicz and colleagues, 2021), though the classical pharmacological targets of PYY are the Y1/Y2/Y4/Y5 receptors.

Open questions

  • Whether a Y2R-selective PYY analog can be developed that retains anorexigenic potency without the nausea liability seen with PYY(3-36) at pharmacological doses
  • Whether the elevated PYY observed after bariatric surgery is causal in sustained weight loss or epiphenomenal
  • Whether the species-variant sequence stored here (Ser at position 3 rather than human Ile) is functionally equivalent to human PYY
  • Oral or stable long-acting PYY formulations have not been validated in late-stage human trials
Hypotheses4 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

Has PYY been incorrectly matched to a receptor it does not normally bind, and should it instead point to the Y2 receptor that mediates its satiety effects?

Correcting this annotation would ensure that any drug-discovery or research effort using this database is working toward the right biological target, avoiding wasted experiments chasing a false receptor interaction.

The hypothesis
The NPBWR1 annotation for PYY is erroneous, and PYY's dominant physiological binding target is the Y2 receptor (NPY2R), with the high ipTM=0.878 reflecting the structure-prediction model being run against the wrong receptor; the actual PYY:Y2R complex would yield substantially higher interface confidence.
Why it’s plausible
PYY (YPSKPEAPGEDASPEELNRYYASLRHYLNLVTRQRY) is a canonical member of the NPY/PYY/PP peptide family whose documented receptors are Y1, Y2, Y4, and Y5 (IUPHAR nomenclature). The readme explicitly states PYY circulates as PYY(1-36) binding broad NPY-family receptors and PYY(3-36) selectively activating Y2 to reduce food intake. NPBWR1 (neuropeptide B/W receptor 1) is the receptor for the structurally unrelated neuropeptides B and W, not for NPY-family peptides. The literature snippets included reference NPB, NPW, and NPBWR1 in adrenal contexts, suggesting a database cross-contamination between NPY-family and NpBW-family entries. The Grandt et al. (1994) work cited in the readme establishes Y2 as the primary truncated-PYY receptor.
Why it matters
If confirmed, this finding indicates a systematic annotation error in the peptide database that would propagate to any downstream analysis trusting the NPBWR1 annotation for PYY, necessitating correction before autonomous research-swarm hypotheses can be reliably generated for this entry.
Plausibility.90
Novelty.50
Impact.75
Basis · grounding3 computed/notes
[1]
noteExplicitly states PYY acts via 'NPY-family receptors' Y1/Y2/Y4/Y5; PYY(3-36) 'selectively activates the Y2 receptor'; no mention of NPBWR1 in functional description
[2]
sourceLiterature snippet concerns NPB, NPW, and NPBWR1 in adrenal cortex/medulla, structurally and functionally distinct from PYY; presence in PYY snippet set suggests database cross-contamination
[3]
sequenceYPSKPEAPGEDASPEELNRYYASLRHYLNLVTRQRY, 36aa, PP-fold family signature (C-terminal TRQRY); no structural homology to neuropeptide B or W sequences which are shorter and structurally distinct
openupdated 2026-06-05

If PYY and GLP-1 target two different but cooperating hunger circuits in the brain, would using both together cause more weight loss than the simple sum of their individual effects?

A synergistic PYY plus GLP-1 combination drug could achieve greater weight loss at lower doses, potentially reducing the nausea and other side effects that currently limit GLP-1 therapy for millions of people.

The hypothesis
Co-formulation of PYY(3-36) with GLP-1 receptor agonists produces supra-additive appetite suppression because PYY acts via Y2 receptor in the arcuate nucleus to inhibit NPY/AgRP neurons while GLP-1 simultaneously activates POMC neurons, engaging complementary and non-overlapping hypothalamic satiety circuits.
Why it’s plausible
The readme notes PYY is co-localized with GLP-1 in intestinal L cells, and both are co-secreted postprandially. GLP-1 agonists (semaglutide, tirzepatide) are the dominant current obesity therapies but reach a satiety ceiling. PYY acts specifically at Y2 receptors on NPY/AgRP neurons (inhibitory), while GLP-1 activates POMC neurons (excitatory), representing genuinely complementary mechanisms. Supra-additivity (synergy) rather than mere additivity would be expected because the two pathways converge on energy balance via non-overlapping first-order targets, as in classical pharmacological synergy models.
Why it matters
Confirmed synergy would provide the mechanistic rationale for a fixed-dose GLP-1/PYY combination that achieves greater weight loss than either alone at lower individual doses, reducing dose-dependent side effects of each component.
Plausibility.65
Novelty.40
Impact.75
Basis · grounding3 computed/notes
[1]
notePYY 'co-localised with glucagon-like peptide-1 (GLP-1) in the L cells of the gastrointestinal mucosa', physiological co-secretion suggests co-evolved complementarity
[2]
sequenceYPSKPEAPGEDASPEELNRYYASLRHYLNLVTRQRY: Y2-receptor-targeting NPY-family peptide; Y2 on arcuate NPY/AgRP neurons is the canonical first-order target, mechanistically distinct from GLP-1R on POMC neurons
[3]
sourcePYY physiology review contextualizing its role in satiety circuits and postprandial release patterns
openupdated 2026-06-05

Could PYY activate the same brain circuits its close relative NPY uses to buffer stress, reducing the urge to drink alcohol when under pressure?

If true, this would open an entirely new use for PYY-based molecules in treating alcohol use disorder, especially the stress-relapse subtype that is notoriously hard to manage with existing medicines.

The hypothesis
PYY suppresses stress-induced alcohol craving via Y2 receptor activation in the locus coeruleus, because Y2 receptors in that brainstem nucleus gate norepinephrine release and stress-induced reinstatement of reward-seeking, mechanisms independent of PYY's gut-satiety role.
Why it’s plausible
NPY and its family members, including PYY, have documented roles in stress resilience and addiction. The locus coeruleus expresses Y2 receptors and is a primary site of norepinephrine synthesis. Stress-induced reinstatement of drug and alcohol seeking is driven in part by norepinephrine release from locus coeruleus projections to the prefrontal cortex and bed nucleus of the stria terminalis. PYY(3-36) reaching the brain after peripheral release, or centrally administered PYY, could dampen this axis via Y2-mediated inhibition of LC firing. This is analogous to NPY's established anxiolytic and anti-addiction role.
Why it matters
PYY-based Y2 agonists targeting stress-alcohol craving would represent a gut-hormone-derived non-opioid pharmacotherapy for alcohol use disorder, a condition with very limited current treatment options.
Plausibility.45
Novelty.65
Impact.65
Basis · grounding3 computed/notes
[1]
notePYY belongs to the NPY family; NPY is a well-established stress-buffer and anti-anxiety neuropeptide in the brain; PYY and NPY share Y2 receptor as primary target
[2]
sourcePYY physiology including central nervous system effects discussed in the context of NPY-family neuropeptide biology
[3]
sequenceYPSKPEAPGEDASPEELNRYYASLRHYLNLVTRQRY: NPY-family PP-fold structure with C-terminal TRQRY motif shared with NPY, consistent with shared receptor pharmacology at Y2 in brain regions
openupdated 2026-06-05

Does swapping isoleucine (human) for serine (non-human) at position 3 of PYY weaken how strongly it activates the Y2 satiety receptor?

If this swap matters for receptor potency, it helps researchers choose the right animal model for PYY satiety studies and guides the design of PYY-based obesity drugs tuned for human receptor pharmacology.

The hypothesis
The Ser at position 3 of this PYY sequence (YPSKPEAPGEDASPEELNRYYASLRHYLNLVTRQRY) relative to Ile3 in human PYY represents a species-variant that weakens Y2 receptor binding by removing a hydrophobic contact, explaining why the PYY(3-36) form is less potent in non-human species that carry Ser3.
Why it’s plausible
The readme flags that 'position 3 reads Ser in this entry, whereas human PYY carries Ile at that position,' identifying this as a likely non-human sequence variant. In PYY(3-36), positions 3-5 (IleXxx in human) sit at the newly exposed N-terminus after DPP-IV cleavage, directly influencing Y2 receptor selectivity. Replacing the hydrophobic Ile with the polar Ser would reduce the hydrophobic N-terminus of PYY(3-36) and could alter Y2 binding affinity, providing a molecular explanation for any interspecies differences in DPP-IV-dependent PYY satiety signaling.
Why it matters
Understanding how Ser3 vs Ile3 modulates Y2 binding across species is relevant both for interpreting animal-model data and for engineering PYY-based satiety drugs with optimized human-Y2 affinity.
Plausibility.55
Novelty.50
Impact.50
Basis · grounding3 computed/notes
[1]
noteExplicitly flags 'position 3 reads Ser in this entry, whereas human PYY carries Ile at that position', confirming species variant
[2]
sequenceYPSKPEAPGEDASPEELNRYYASLRHYLNLVTRQRY: Ser at position 3; human PYY has Ile at this position; in PYY(3-36) this position becomes the N-terminal residue after DPP-IV cleavage, directly presented to Y2
[3]
sourcePYY satiety biology discussed in physiological context
details expand to inspect
full evidence table2 metrics
metricvaluetool
ipTM 0.8776953220367432 boltz-2
ranking score 0.8432674407958984 boltz-2
structural qualityopenfold3
metricvaluenote
gpde0.623global PDE — lower = better
disorderNaNfraction disordered
3-letter notation
Tyr-Pro-Ser-Lys-Pro-Glu-Ala-Pro-Gly-Glu-Asp-Ala-Ser-Pro-Glu-Glu-Leu-Asn-Arg-Tyr-Tyr-Ala-Ser-Leu-Arg-His-Tyr-Leu-Asn-Leu-Val-Thr-Arg-Gln-Arg-Tyr
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). Peptide YY: gut hormone that tells the brain you're full (pep-10717, v1). PeptideModel. https://peptidemodel.com/card/pep-10717
@peptide{pep10717,
  sequence = {YPSKPEAPGEDASPEELNRYYASLRHYLNLVTRQRY},
  target   = {npbwr1},
  author   = {peptidemodel},
  year     = {2026},
  status   = {synthesized}
}
related peptides 5 by signal overlap
clinical trials 398 on ct.gov · 3 on EUCTR · checked 2026-05-09
ct.gov trials 398
with results 22
EUCTR 3
PubMed RCT 42
by phase
1phase 11phase 28no phase
by status
7completed2recruiting1terminated
references 8 papers
discussion no comments
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peptidemodel.com CC-BY-SA-4.0 research only · not for human use