pe
pep-10655 v1 CC-BY-SA-4.0

Peptide YY [3-36]: gut 'I'm full' hormone fragment

A natural gut hormone fragment released after eating that travels to the brain and reduces appetite; the rabbit form is used as a lab research tool.

statussynthesized targetNPBWR1 length34 aa refs5
snapshot sparse 15% confidence
Class
Endogenous peptide fragment
Status
No approved therapeutic status identified
Best-supported effect
Characterized as a naturally occurring truncated form of peptide YY in rabbit; no functional or therapeutic effect established in this card's source
Main caveat
Source file contains sequence and a single species-characterization reference only; no efficacy, receptor, or clinical data are attached
status 4 / 5
prediction metrics boltz-2 2.2.1
ipTM0.934
pTM0.911
avg pLDDT85.0
ranking score0.867
STRUCTURE · PEP-10655 × NPBWR1
ranking0.867
target interface 4.5Å peptide drag rotate · ctrl+scroll zoom · right-click pan
boltz-2 2.2.1 · mmCIF ↓ download
sequence34 aa
15101520253034
SKPEAPGEDASPEELNR YYASLRHYLNLVTRQRY
overview readme

What this is

Peptide YY [3-36] (PYY[3-36]) is a natural gut hormone fragment that acts as a satiety signal — it tells the brain that the body has eaten enough. The peptide is generated from full-length peptide YY (PYY[1-36]) when the enzyme dipeptidyl peptidase IV (DPP-IV) cleaves the two N-terminal amino acids after the full-length form is secreted into circulation. The sequence stored here — SKPEAPGEDASPEELNRYYASLRHYLNLVTRQRY — is the rabbit form of PYY[3-36]; Grandt and colleagues (1994) were the first to characterize both PYY(1-36) and PYY(3-36) in rabbit intestinal tissue, establishing that rabbit PYY differs from porcine PYY by two amino acid substitutions and from human PYY by one, making the rabbit a useful model for studying PYY biology. PYY belongs to the neuropeptide Y (NPY) peptide family, and its name reflects the tyrosine (single-letter code: Y) residues at both its N- and C-termini — though the active fragment PYY[3-36] retains only the C-terminal tyrosine.

History

PYY was originally isolated from porcine intestinal extracts in 1980. Grandt and colleagues (1994) later characterized two molecular forms — the full-length PYY(1-36) and the truncated PYY(3-36) — in rabbit tissue, purifying the peptide from intestinal mucosa and determining its primary structure. This rabbit characterization was significant because rabbit tissues had been widely used to map PYY receptor subtypes even though the rabbit sequence was still unknown at the time. The discovery that DPP-IV proteolysis converts PYY[1-36] into PYY[3-36] shifted the receptor pharmacology dramatically: the full-length form is a non-selective agonist across the NPY receptor family, whereas the truncated fragment is a highly selective agonist at the Y2 receptor (Y2R/NPY2R), the subtype most relevant to appetite suppression. Interest in PYY[3-36] as a potential obesity therapy intensified in the early 2000s following studies showing that peripheral infusion of postprandial concentrations of the peptide significantly reduced food intake in both lean and obese humans (Karra and colleagues 2009).

What it does

After a meal, L-cells in the distal small intestine and colon release PYY[3-36] in proportion to the caloric content of the food consumed. Plasma levels begin rising within minutes of eating and remain elevated for several hours, helping to prolong the feeling of fullness (Karra and colleagues 2009; Vincent and colleagues 2008). The peptide acts centrally — primarily in the hypothalamus — and peripherally via the vagus nerve to reduce appetite and slow the rate at which the stomach empties. In humans, infusion of PYY[3-36] at normal postprandial concentrations has been shown to significantly reduce food intake over the following 24 hours; notably, obese individuals retain sensitivity to this effect, distinguishing PYY from leptin, to which obese subjects are typically resistant (Karra and colleagues 2009). Beyond appetite, Persaud and colleagues (2014) have reviewed evidence linking PYY to bone metabolism, immune function, and cardiovascular regulation, suggesting a broader physiological portfolio than appetite regulation alone.

Evidence

  • Human: Peripheral infusion of PYY[3-36] reduces food intake in both lean and obese human subjects, with obese individuals showing intact Y2R-mediated anorectic responses (Karra and colleagues 2009; Batterham and colleagues reviewed therein). A small clinical study reported that high-dose infusions caused nausea in a majority of participants, limiting the dose range at which the peptide is well tolerated. Combined administration with GLP-1(7-36) amide reduced food intake additively in overweight humans (Silva and colleagues 2012).
  • Animal: Y2 receptor knockout mice are fully resistant to the anorectic effect of PYY[3-36], establishing the Y2R as the necessary mediator; PYY-deficient mice develop obesity that is reversed by PYY[3-36] replacement (Karra and colleagues 2009). Rodent models of diet-induced obesity show reduced food intake and weight after peripheral PYY[3-36] administration.
  • In vitro: Electrophysiology studies in the arcuate nucleus demonstrate that PYY[3-36] directly inhibits the firing of NPY/AgRP neurons via postsynaptic Y2 receptors and activates POMC neurons, shifting the hypothalamic balance from hunger-promoting to satiety-promoting signalling (Karra and colleagues 2009).

Known effects

  • Appetite suppression — Preclinical and human studies; requires intact Y2 receptor signalling
  • Gastric emptying delay — Documented in human studies at physiological concentrations (Vincent and colleagues 2008)
  • Postprandial satiety prolongation — Physiological role; levels rise with meal caloric content (Karra and colleagues 2009)
  • Additive satiety with GLP-1 — Human infusion data; complementary hypothalamic pathways (Silva and colleagues 2012)
  • Possible roles in bone, immune, and cardiovascular regulation — Under active investigation; reviewed by Persaud and colleagues (2014)

Safety signals

Dose-dependent nausea is the primary adverse effect reported in human infusion studies. At higher infusion rates, a majority of subjects experienced nausea severe enough to require termination of the infusion; lower doses were generally better tolerated (Karra and colleagues 2009). An intranasal formulation developed for obesity treatment showed gastrointestinal adverse events as the main tolerability concern in clinical testing, and the Phase 2 trial of a nasal spray formulation did not meet its weight-loss primary endpoint. A long-acting PYY[3-36] analogue studied in combination with semaglutide (2025 clinical data) showed modest additional weight loss but significant GI tolerability issues at higher doses. PYY[3-36] is not approved as a drug in any jurisdiction. No human trials have been completed for the rabbit sequence variant specifically; most clinical work has used the human/porcine sequence.

Regulatory status

  • US: Not FDA-approved. Investigational only. No IND-active programme known for the rabbit sequence specifically.
  • EU: Not EMA-approved.
  • WADA: PYY[3-36], as a peptide hormone with appetite-modifying effects, falls within the class of peptide hormones subject to WADA's general prohibition framework; specific listing status should be verified in the current WADA Prohibited List.

Related peptides

  • PYY[1-36] — the full-length precursor; non-selective Y-receptor agonist; converted to PYY[3-36] by DPP-IV in circulation
  • Neuropeptide Y (NPY) — the family prototype; shares the C-terminal "PP-fold" structure; endogenous orexigenic peptide acting at Y1 and Y5 receptors
  • Pancreatic Polypeptide (PP) — a third NPY-family member released postprandially from the pancreas; Y4-receptor selective; reviewed alongside PYY[3-36] in appetite biology (Silva and colleagues 2012; Persaud and colleagues 2014)
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 2026-06-11

Is the receptor listed for this peptide a mistake, and does PYY[3-36] actually work through the well-known Y2 receptor?

If the annotation is wrong, correcting it would point research at the right target. The NPBWR1 label here looks like an automated mis-assignment shared across several PYY and NPY family entries; the published references all describe PYY[3-36] as a selective Y2 receptor agonist.

The hypothesis
The annotated target NPBWR1 for rabbit PYY[3-36] is incorrect; the primary receptor mediating its satiety and gastric-emptying actions is NPY Y2 receptor (NPY2R), and the high complex ipTM (0.934) reflects structural compatibility with NPY2R rather than NPBWR1.
Why it’s plausible
PYY[3-36] is canonically a selective NPY Y2 receptor agonist, and DPP-IV cleavage of the N-terminal SK precisely removes the residues that confer Y1/Y5 binding while preserving the C-terminal RQRY motif required for Y2 selectivity. NPBWR1 is the neuropeptide B/W receptor, a phylogenetically distinct GPCR whose known endogenous ligands are neuropeptide B and neuropeptide W, not PP-fold peptides. An ipTM of 0.934 in a Boltz-2 run against the annotated receptor does not by itself validate that annotation.
Why it matters
If the target annotation is wrong, any structure-based drug design or downstream hypothesis built on NPBWR1 binding is misguided. Confirming NPY2R as the true receptor is essential before using this card to prioritize therapeutic leads or interpret the structural data.
Plausibility.90
Novelty.25
Impact.80
Basis · grounding3 computed/notes
[1]
noteREADME identifies PYY[3-36] as a satiety signal acting on the NPY peptide family receptor system; DPP-IV cleavage generates the fragment that shifts pharmacology toward Y2 selectivity.
[2]
structureBoltz-2 complex ipTM=0.934 for the annotated NPBWR1 complex; high confidence could indicate correct fold-level docking but does not confirm biological target identity.
[3]
sequenceC-terminal RQRY motif is the hallmark NPY-family Y2 binding motif; the SK N-terminus lost by DPP-IV cleavage is the region responsible for Y1/Y5 engagement.
openupdated 2026-06-11

Could this appetite-suppressing peptide also affect patients whose stomachs empty too slowly, such as people with diabetes-related gastroparesis?

PYY[3-36] is documented to slow stomach emptying, and Y2 receptors are present on gut nerves, so a peripheral motility effect is plausible. Whether it could help or worsen a specific motility disorder is unknown and would need direct study, but it points to a question worth investigating beyond appetite.

The hypothesis
PYY[3-36] may have therapeutic utility in postoperative ileus and gastroparesis beyond its established satiety role, because its documented gastric emptying delay acts through enteric Y2 receptors on smooth muscle rather than solely through central appetite circuits, and this peripheral mechanism is independent of the CNS satiety pathway.
Why it’s plausible
One literature snippet explicitly reports that intramuscular PYY3-36 injection delays gastric emptying. Gastroparesis and postoperative ileus involve dysregulated gastric motility, and Y2 receptors are expressed on enteric neurons and smooth muscle throughout the gut. If the motility effect can be isolated from appetite suppression (e.g., by dose titration or tissue-targeted delivery), PYY[3-36] or analogs could treat motility disorders where current prokinetic options are limited.
Why it matters
Gastroparesis affects a large diabetic and post-surgical population with few effective treatments. Repurposing a well-characterized natural peptide for motility modulation would be faster to develop than a de novo drug, and the existing safety data from obesity trials would support bridging studies.
Plausibility.65
Novelty.55
Impact.65
Basis · grounding2 papers · 1 computed/note
[1]
paper
Explicitly reports intramuscular PYY3-36 injection effectively delays gastric emptying in rodents, directly supporting a peripheral motility mechanism beyond appetite suppression.
doi: 10.1136/jcp.2007.048488
[2]
noteREADME establishes PYY[3-36] as a gut-secreted peptide acting on the NPY family receptor system, consistent with peripheral enteric expression of Y2 receptors on smooth muscle and enteric neurons.
[3]
paper
Review context for gut hormone analogs discusses clinical translation challenges, implying the therapeutic space for gut-motility peptide drugs is under active development.
doi: 10.5009/gnl.2012.6.1.10
openupdated 2026-06-11

Is the rabbit version of this satiety peptide close enough to the human version that the receptor it acts on responds the same way?

The single difference between the rabbit and human forms sits at the far N-terminal end, away from the C-terminal region that contacts the Y2 receptor, so the two forms may be similar at that receptor. If borne out, this would help interpret older rabbit-based studies, though it has not been directly tested.

The hypothesis
Rabbit PYY[3-36] has equivalent or superior Y2 receptor affinity compared to human PYY[3-36] due to its single amino acid difference being located outside the core receptor-contact residues, making the rabbit sequence a viable surrogate for human clinical studies when human peptide supply is limited, and supporting its direct use in rabbit-model preclinical safety studies without species mismatch concerns.
Why it’s plausible
The README notes that rabbit tissues were widely used to map PYY receptor subtypes before the rabbit sequence was known. If the single amino acid difference is in the N-terminal or mid-loop region and not in the C-terminal RQRY pharmacophore or the amphipathic helix, it would not be predicted to alter Y2 affinity substantially. Confirming this would validate decades of rabbit-model pharmacology data and streamline IND-enabling studies.
Why it matters
Cross-species sequence equivalence at the receptor interface is a regulatory and practical concern when translating PYY-based therapies from rabbit preclinical models to human trials. Establishing that the rabbit and human forms are pharmacologically equivalent at Y2 reduces uncertainty in dose extrapolation.
Plausibility.70
Novelty.15
Impact.40
Basis · grounding1 paper · 2 computed/notes
[1]
noteREADME states rabbit tissues were widely used to map PYY receptor subtypes even before the rabbit sequence was known, implying assumed pharmacological equivalence that has not been formally confirmed.
[2]
sequenceC-terminal RQRY is conserved and constitutes the primary Y2 pharmacophore; the single substitution relative to human is elsewhere in the 34 aa sequence, predicted to have minimal impact on Y2 contact.
[3]
paper
PYY3-36 intramuscular injection causes measurable weight loss in rodents (1.9% average), establishing that the peptide is active across species and supporting interspecies pharmacological extrapolation.
doi: 10.1136/jcp.2007.048488
details expand to inspect
full evidence table2 metrics
metricvaluetool
ipTM 0.9341727495193481 boltz-2
ranking score 0.8670646548271179 boltz-2
3-letter notation
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 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 [3-36]: gut 'I'm full' hormone fragment (pep-10655, v1). PeptideModel. https://peptidemodel.com/card/pep-10655
@peptide{pep10655,
  sequence = {SKPEAPGEDASPEELNRYYASLRHYLNLVTRQRY},
  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 5 papers
discussion no comments
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