pe
pep-10712 v1 CC-BY-SA-4.0

Peptide YY: gut fullness hormone (canine/mouse/pig/rat forms)

A natural gut hormone released after eating that tells the brain you're full; studied in animals to understand appetite and stress; not a drug.

statussynthesized targetNPBWR1 length36 aa refs13
status 4 / 5
prediction metrics boltz-2 2.2.1
ipTM0.884
pTM0.897
avg pLDDT82.6
ranking score0.838
STRUCTURE · PEP-10712 × NPBWR1
ranking0.838
target interface 4.5Å peptide drag rotate · ctrl+scroll zoom · right-click pan
boltz-2 2.2.1 · mmCIF ↓ download
sequence36 aa
1510152025303536
YPAKPEAPGEDASPEELS RYYASLRHYLNLVTRQRY
overview readme

What this is

Peptide YY (PYY) is a gut hormone released after eating that tells the brain to stop eating — one of the body's primary "fullness" signals. It is produced mainly by specialized cells (L-cells) in the lower small intestine and colon, and it is released in proportion to the calorie content of a meal. The name comes from the presence of tyrosine (one-letter code: Y) at both the N- and C-termini of the 36-amino-acid chain. PYY was first isolated from porcine intestinal tissue by Tatemoto (1982) and is highly conserved across mammals; the stored sequence here represents the canonical 36-residue backbone shared across canine, mouse, porcine, and rat species. The active molecule carries a C-terminal tyrosine amide (–NH₂) that is not visible in the standard one-letter sequence but is required for full receptor binding activity (Tatemoto 1982).

History

Kazuhiko Tatemoto isolated PYY from extracts of porcine upper intestinal tissue in 1982, using a novel chemical assay that detected the unusual C-terminal amide structure (Tatemoto 1982, PNAS). He noted the sequence's homology to pancreatic polypeptide (PP) and proposed that PYY and PP together form a new peptide family — what is now called the PP-fold (or NPY) family. That family also includes neuropeptide Y (NPY), and all three share a characteristic hairpin-loop tertiary structure. The initial report identified PYY as a candidate gut hormone that inhibits pancreatic exocrine secretion. Over the following decades, research expanded PYY's known roles to appetite regulation, gastrointestinal motility, and energy homeostasis (Chaudhri and colleagues 2006; Vincent and colleagues 2008). In 2002, Batterham and colleagues demonstrated in Nature that the circulating fragment PYY(3–36) acts via the hypothalamic arcuate nucleus to reduce food intake by 33% in human volunteers — establishing PYY as a major target for obesity research.

What it does

After a meal, PYY is secreted from L-cells into the bloodstream and acts to slow digestion and suppress appetite. It inhibits gastric acid secretion, slows gastric emptying and intestinal transit (the "ileal brake" effect), and reduces pancreatic enzyme and bicarbonate secretion — actions that collectively help pace nutrient absorption (Chey and colleagues 2001; Chaudhri and colleagues 2006). Simultaneously, circulating PYY signals the hypothalamus to dampen appetite. The predominant circulating form, PYY(3–36), is generated when the enzyme DPP-IV cleaves the N-terminal Tyr-Pro dipeptide from the full-length PYY(1–36); this truncation shifts receptor selectivity heavily toward the Y2 subtype and is the form responsible for the central appetite-suppressing effect (Vincent and colleagues 2008; Silva and colleagues 2012). Fasting and postprandial PYY levels are consistently lower in obese individuals than in lean controls, pointing to a blunted satiety signal as a possible contributor to excess food intake (Vincent and colleagues 2008).

Evidence

  • Human: Intravenous infusion of postprandial concentrations of PYY(3–36) significantly decreased appetite and reduced 24-hour food intake by 33% in lean and obese volunteers (Batterham and colleagues 2002, cited in Vincent and colleagues 2008 and Silva and colleagues 2012). A Phase II randomized placebo-controlled trial of intranasal PYY(3–36) in obese adults by Gantz and colleagues (2007, JCEM) found no statistically significant weight loss versus placebo after 12 weeks at the 200 µg dose; the 600 µg dose arm was largely discontinued due to nausea and vomiting. No PYY-based therapy is currently approved.
  • Animal: Peripheral injection of PYY(3–36) inhibits food intake in rodents through Y2 receptor-dependent mechanisms; the effect is absent in Y2-receptor-null mice (cited in Vincent and colleagues 2008). Postprandial PYY levels rise markedly after Roux-en-Y gastric bypass in animal models, paralleling the appetite reduction seen after surgery.
  • In vitro: PYY(1–36) and PYY(3–36) show distinct receptor-subtype binding profiles across the Y-receptor family; PYY(1–36) binds Y1, Y2, and Y5 subtypes, while the truncated PYY(3–36) preferentially targets Y2 (Silva and colleagues 2012).

Known effects

  • Appetite suppression — Emerging/Preclinical-to-Phase II; mediated by Y2 receptor signaling in the arcuate nucleus
  • Inhibition of pancreatic exocrine secretion — Mechanistic/Preclinical; blocks secretin- and CCK-stimulated enzyme and bicarbonate output (Tatemoto 1982; Chey and colleagues 2001)
  • Gastric emptying delay / ileal brake — Mechanistic; reduces gastric motility and intestinal transit rate (Chaudhri and colleagues 2006)
  • Reduced postprandial food intake — Phase II (human infusion studies); 33% reduction in 24-hour caloric intake in human infusion studies (cited in Vincent and colleagues 2008)
  • Elevated post-bariatric surgery levels — Observational; circulating PYY rises substantially after Roux-en-Y gastric bypass, potentially contributing to post-surgical satiety (Silva and colleagues 2012)

Safety signals

The clinical safety record for exogenous PYY is limited. In the Gantz and colleagues (2007) Phase II intranasal trial, nausea and vomiting were the primary adverse effects; 59% of participants in the highest-dose arm (600 µg three times daily) discontinued due to these effects. The 200 µg arm was better tolerated but inefficacious. No long-term safety data from approved human use exists, as no PYY-based drug has cleared regulatory review. The dose-dependent emetic profile has been a key obstacle for intranasal and subcutaneous development programmes.

Regulatory status

  • US: Not approved. Investigational only. No PYY-based drug has completed Phase III trials or received FDA review.
  • EU: Not approved. Not on the EMA product database.
  • WADA: Not listed on the prohibited list as of 2026. Endogenous peptide hormones occupy a regulatory grey zone; classification may change if efficacious formulations reach development.

Related peptides

PYY belongs to the PP-fold family alongside neuropeptide Y and pancreatic polypeptide, which share the hairpin tertiary structure and act through overlapping Y-receptor subtypes. For gut-derived satiety hormones co-released from L-cells, see also GLP-1 receptor agonists such as semaglutide and liraglutide, which act through a distinct receptor but are co-secreted with PYY postprandially and have reached regulatory approval for obesity and type-2 diabetes (Silva and colleagues 2012; Chaudhri and colleagues 2006).

Hypotheses2 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

Does PYY only activate the NPBWR1 stress-linked receptor when it carries the amide chemical tag on its tail, while the satiety Y2 receptor accepts either form?

If true, defects in the enzyme that adds this amide tag could quietly shift PYY's function, potentially contributing to eating disorders or chronic stress conditions in a way that would be missed by studies that only measure total PYY levels.

The hypothesis
The C-terminal amide on Tyr36 of PYY is required for NPBWR1 engagement but not for Y2 engagement, such that non-amidated recombinant PYY(1-36) retains Y2-mediated satiety activity while losing NPBWR1 signalling, creating a built-in pharmacological switch based on post-translational modification.
Why it’s plausible
The readme for pep-10712 explicitly states that the C-terminal tyrosine amide is required for full receptor binding activity but is not visible in the raw sequence, noting it is essential for the PP-fold family. Amide-dependent binding is differentially required across receptor subtypes in neuropeptide families: in the NPY family, Y1 and Y2 show different sensitivities to C-terminal modification. If NPBWR1, which evolved to bind NPB/NPW (which carry C-terminal amides), is more stringently amide-dependent than Y2, then amidation state becomes a post-translational selectivity gate.
Why it matters
If amidation differentially gates NPBWR1 vs. Y2 signalling, then incompletely processed PYY in disease states (e.g. alpha-amidating monooxygenase deficiency) would have an altered receptor selectivity profile, potentially contributing to metabolic or stress dysregulation.
Plausibility.40
Novelty.55
Impact.45
Basis · grounding1 paper · 2 computed/notes
[1]
noteExplicitly states: the active molecule carries a C-terminal tyrosine amide required for full receptor binding activity; the Tatemoto 1982 PNAS paper identified this amide as structurally defining.
[2]
paper
Tatemoto's original PYY characterisation noted the C-terminal amide structure as critical and defining for the PP/PYY peptide family receptor interactions.
doi: 10.1073/pnas.79.8.2514
[3]
sequenceRaw sequence ends in ...TRQRY without showing amidation; amide on Tyr36 is a known post-translational modification that could differentially affect NPBWR1 vs. Y2 binding.
openupdated 2026-06-05

Does PYY reduce damaging enzyme secretion from the pancreas through both its known receptor and the NPBWR1 receptor, making it more effective than single-receptor approaches?

If true, PYY or a stable version of it could be developed as a treatment for pancreatitis, a painful and potentially life-threatening condition with few good medical therapies available today.

The hypothesis
Rodent/canine PYY(1-36) reduces post-prandial pancreatic exocrine secretion via a NPBWR1-dependent pathway in the pancreas, separate from its original PP-family activity of inhibiting pancreatic secretion via PP receptors, suggesting PYY(1-36) as a candidate to reduce pathological enzyme hypersecretion in pancreatitis.
Why it’s plausible
Tatemoto's original 1982 PYY characterisation (10.1073/pnas.79.8.2514) demonstrated that PYY (200 pmol/kg) markedly inhibits secretin- and CCK-stimulated pancreatic protein, fluid, and bicarbonate secretion in the anaesthetised cat. NPBWR1 mRNA expression has been found in multiple endocrine-relevant tissues including adrenal glands. If NPBWR1 is also expressed in pancreatic acinar or ductal cells, PYY's pancreatic inhibitory action could involve both the canonical PP-family receptor mechanism and an NPBWR1-dependent component, making PYY(1-36) dual-mechanism in the pancreas.
Why it matters
Pancreatitis involves pathological hypersecretion of pancreatic enzymes. A dual-mechanism inhibitor of pancreatic secretion based on the endogenous PYY scaffold could offer a more robust suppression of enzyme secretion than Y4-selective PP analogues currently under investigation.
Plausibility.35
Novelty.50
Impact.45
Basis · grounding1 paper · 2 computed/notes
[1]
paper
Figure 8 shows PYY at 200 pmol/kg markedly suppresses secretin- and CCK-stimulated pancreatic secretion of protein, fluid, and bicarbonate in the cat, establishing pancreatic exocrine inhibition as a primary PYY action.
doi: 10.1073/pnas.79.8.2514
[2]
structureipTM=0.884 for rodent PYY/NPBWR1 supports binding plausibility; if NPBWR1 is expressed in pancreatic tissue, this could contribute to the observed pancreatic inhibition.
[3]
noteNotes the initial report identified PYY as inhibiting pancreatic exocrine secretion; expanded roles to include motility and energy balance came later, suggesting early pancreatic action deserves re-examination with modern receptor biology.
details expand to inspect
full evidence table2 metrics
metricvaluetool
ipTM 0.8840794563293457 boltz-2
ranking score 0.8378406763076782 boltz-2
3-letter notation
Tyr-Pro-Ala-Lys-Pro-Glu-Ala-Pro-Gly-Glu-Asp-Ala-Ser-Pro-Glu-Glu-Leu-Ser-Arg-Tyr-Tyr-Ala-Ser-Leu-Arg-His-Tyr-Leu-Asn-Leu-Val-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). Peptide YY: gut fullness hormone (canine/mouse/pig/rat forms) (pep-10712, v1). PeptideModel. https://peptidemodel.com/card/pep-10712
@peptide{pep10712,
  sequence = {YPAKPEAPGEDASPEELSRYYASLRHYLNLVTRQRY},
  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 13 papers
[2]
Neuropeptidomics of the Rat Habenular Nuclei
Yang, N. et al. Journal of Proteome Research 2018
supporting
[5]
Gastrointestinal hormones regulating appetite
Chaudhri, O. et al. Philosophical Transactions of the Royal Society B: Biological Sciences 2006
supporting
[6] supporting
[10] supporting
[12]
Efficacy and Safety of Intranasal Peptide YY3–36 for Weight Reduction in Obese Adults
Gantz, I. et al. The Journal of Clinical Endocrinology & Metabolism 2007
supporting
[13]
The satiety hormone peptide YY as a regulator of appetite
Vincent, R. et al. Journal of Clinical Pathology 2008
supporting
discussion no comments
sign in to comment
peptidemodel.com CC-BY-SA-4.0 research only · not for human use