pe
pep-10604 v1 CC-BY-SA-4.0

PYY(3-36): natural fullness hormone released after eating

A gut hormone the body makes after a meal to tell the brain you're full; studied as a possible treatment for obesity, but not yet an approved drug.

statussynthesized targetNPY2R length34 aa refs12
status 4 / 5
prediction metrics boltz-2 1.0
ipTM0.942
pTM0.924
avg pLDDT71.9
ranking score0.763
STRUCTURE · PEP-10604 × NPY2R
ranking0.763
target interface 4.5Å peptide drag rotate · ctrl+scroll zoom · right-click pan
boltz-2 1.0 · mmCIF ↓ download
sequence34 aa
15101520253034
IKPEAPGEDASPEELNR YYASLRHYLNLVTRQRY
overview readme

What this is

PYY(3-36) — also written as peptide YY(3-36) or PYY3-36 — is a 34-amino-acid gut hormone fragment that the body naturally produces after eating. It is released by specialized cells lining the lower small intestine and colon, travels through the bloodstream to the brain, and signals that a meal has been consumed. The active fragment is generated from the full 36-amino-acid peptide YY by the enzyme DPP-4, which trims two residues from the N-terminus; the resulting PYY(3-36) is the form that drives satiety signaling (Karra et al. 2009; Ballantyne 2006). Unlike some gut peptides that have been turned into approved drugs, no PYY(3-36) product has reached the market — but its central role in the body's own appetite-regulation circuitry makes it a consistent reference point in obesity research and in understanding why bariatric surgery produces lasting weight loss.

History

Peptide YY was isolated in 1982 by Kazuhiko Tatemoto, Mats Carlquist, and Viktor Mutt working from porcine upper intestinal tissue at the Karolinska Institute. Their method targeted peptides with C-terminal tyrosine amides, which led simultaneously to PYY and neuropeptide Y (NPY) from brain tissue; the name referenced the tyrosine (Y) residues at both termini of the 36-amino-acid sequence (Tatemoto and colleagues 1982). For roughly two decades PYY was studied mainly as a regulator of pancreatic secretion and gastrointestinal motility. Its standing as a genuine satiety hormone changed in 2002 when Batterham and colleagues at Imperial College London reported in Nature that peripheral infusion of PYY(3-36) at physiologic postprandial concentrations reduced ad libitum caloric intake by roughly 33% over 24 hours in healthy volunteers (Batterham et al. 2002, Nature; summarized in Karra et al. 2009). A follow-up study published in the New England Journal of Medicine in 2003 extended the finding to obese subjects and showed that postprandial PYY levels were blunted in obesity, suggesting a possible contribution to impaired satiety (Batterham et al. 2003, NEJM; le Roux et al. 2006). These results triggered drug-development programs. An intranasal PYY(3-36) spray developed by Nastech Pharmaceutical (later MDRNA) failed its Phase 2 efficacy endpoint in 2007, with dropout driven by nausea and vomiting at higher doses (peptidelist catalog). Novo Nordisk's long-acting analogue NNC0165-1875, designed for once-weekly dosing as an add-on to semaglutide, reported only modest incremental weight loss in Phase 2 and was discontinued (peptidelist catalog). In parallel, observational and mechanistic work established that Roux-en-Y gastric bypass surgery produces exaggerated postprandial PYY release, sustained for years — a finding cited as one mechanism underlying the durable satiety effects of bariatric surgery (Silva et al. 2012).

What it does

After a meal, intestinal L-cells release PYY(3-36) in proportion to the caloric load — protein and fat are the strongest stimuli. The peptide reaches the brain via the bloodstream and dampens the drive to eat: in infusion studies it consistently reduced how much people ate at a subsequent meal and lowered total caloric intake across the following 24 hours (Karra et al. 2009; le Roux et al. 2006). Beyond appetite suppression, PYY(3-36) slows gastric emptying and inhibits pancreatic exocrine secretion, reinforcing the satiety state from multiple angles (Ballantyne 2006; Vincent et al. 2008). In people with obesity, the postprandial rise in PYY is blunted compared with lean individuals, and this blunting correlates with reduced subjective satiety — the proposed mechanism linking PYY deficiency to impaired appetite control in obesity (le Roux et al. 2006). A separate line of research has found that PYY(1-36) — the full-length form, not PYY(3-36) — is also secreted by Paneth cells in the gut epithelium and functions as an antimicrobial peptide maintaining fungal commensalism; this Paneth-cell role is specific to the full-length form and is not shared by PYY(3-36) (Pierre et al. 2023).

Evidence

  • Human: Physiologic IV infusion of PYY(3-36) at postprandial concentrations reduced food intake in healthy lean and obese volunteers in controlled studies (Karra et al. 2009). Obese subjects show blunted postprandial PYY release associated with reduced satiety (le Roux et al. 2006). An intranasal PYY(3-36) Phase 2 trial (Nastech) failed its weight-loss efficacy endpoint; a long-acting analogue (NNC0165-1875) showed only modest incremental benefit over semaglutide in Phase 2 and was discontinued (peptidelist catalog).
  • Animal: Rodent studies consistently show reduced food intake and body weight gain with peripheral PYY(3-36) administration; Y2 receptor knockout abolishes the effect (summarized in Karra et al. 2009). Primate data in rhesus macaques showed PYY(3-36) inhibited morning but not evening food intake, with associated body-weight reduction (Koegler and colleagues 2005, Diabetes).
  • In vitro / mechanistic: Y2-receptor-mediated inhibition of orexigenic NPY/AgRP neurons in the arcuate nucleus has been characterized as the central anorectic mechanism; functional MRI studies in humans showed PYY(3-36) infusion shifts hypothalamic activity toward a fed-state pattern (Karra et al. 2009). Co-secretion with GLP-1 from L-cells and additive appetite suppression in co-infusion studies provide the mechanistic rationale for combination gut-hormone approaches (Silva et al. 2012).

Known effects

  • Reduced food intake / appetite suppression — Human infusion studies (physiologic doses); effect size roughly 30% caloric intake reduction; Moderate evidence (Karra et al. 2009)
  • Blunted postprandial release in obesity — Observed in human studies; correlates with reduced satiety; the causal direction (driver vs. consequence of obesity) is not settled (le Roux et al. 2006)
  • Slowed gastric emptying — Peripheral effect documented; reinforces satiety signaling (Ballantyne 2006)
  • Inhibition of pancreatic exocrine secretion — Documented peripheral effect (Ballantyne 2006)
  • Elevated levels after bariatric surgery — Exaggerated postprandial PYY release after Roux-en-Y gastric bypass is well-documented and cited as a contributor to durable post-surgical satiety (Silva et al. 2012)
  • Antimicrobial activity (full-length PYY1-36 only) — Paneth-cell PYY1-36 acts as an antimicrobial peptide; this property is absent in PYY(3-36) (Pierre et al. 2023)

Safety signals

Safety data on exogenous PYY(3-36) comes from short-duration infusion studies and the discontinued clinical programs rather than from chronic licensed use. The consistent dose-limiting toxicity across programs has been nausea and vomiting, which narrowed the therapeutic window and contributed to the Nastech Phase 2 dropout and to tolerability constraints in the NNC0165-1875 Phase 2 add-on trial (peptidelist catalog; Karra et al. 2009). Long-term safety, cardiovascular outcomes, and effects of chronic Y2-receptor agonism on bone, pancreatic function, or other organ systems have not been characterized at the level of evidence available for GLP-1 agonists, because no PYY analogue has progressed to chronic licensed use (peptidelist catalog). No FDA-approved or EMA-approved PYY product exists.

Regulatory status

  • US: No FDA-approved PYY or PYY(3-36) product for any indication. Research use under investigational (IND) pathways.
  • EU: No EMA-approved PYY product.
  • WADA: PYY(3-36) is not specifically named on the WADA Prohibited List. WADA category S2 (peptide hormones, growth factors, related substances and mimetics) is written broadly; athletes should seek guidance from their national anti-doping organization before any use (peptidelist catalog).

Mechanism

PYY(3-36) is produced by enteroendocrine L-cells in the distal small intestine and colon, co-secreted with GLP-1 in response to nutrient ingestion. DPP-4 cleaves two residues from the N-terminus of the full-length PYY(1-36), yielding the Y2-receptor-selective active fragment PYY(3-36) (Karra et al. 2009; Ballantyne 2006). In the arcuate nucleus of the hypothalamus, PYY(3-36) acts on Y2 autoreceptors on orexigenic NPY/AgRP neurons, suppressing their activity and thereby disinhibiting downstream anorexigenic POMC neurons — a mechanism that has been characterized as central to the anorectic effect (Karra et al. 2009). Additional sites of action include the vagus nerve and brainstem nuclei (area postrema, nucleus tractus solitarius), consistent with a distributed appetite-suppression circuit (Karra et al. 2009; Vincent et al. 2008). Effects on food intake appear additive with GLP-1 in co-infusion studies, which is the pharmacological basis for interest in combination gut-hormone therapeutics targeting both the GLP-1 receptor and the Y2 receptor (Silva et al. 2012). The stored sequence for this card is the 34-residue PYY(3-36) fragment (positions 3–36 of the full PYY sequence); the native peptide is a linear sequence with no reported lipid conjugation, PEGylation, or cyclization. Endogenous PYY(3-36) has a short plasma half-life, which is why therapeutic development has focused on longer-acting analogues (Karra et al. 2009).

Open questions

  • Why PYY(3-36) drug development has repeatedly failed the tolerability-efficacy tradeoff while GLP-1 agonism succeeded — whether this reflects a fundamentally narrow therapeutic window at Y2, delivery and half-life challenges, or molecule-engineering limitations is not settled (Karra et al. 2009; peptidelist catalog).
  • Whether a next-generation long-acting PYY(3-36) analogue with improved tolerability could add clinically meaningful benefit on top of GLP-1 or dual GLP-1/GIP agonism.
  • Whether blunted postprandial PYY in obesity is a driver of impaired satiety or a consequence of adiposity, altered meal composition, or gut microbiota changes — the causal direction remains unresolved (le Roux et al. 2006).
  • The relative contribution of PYY versus GLP-1 versus other gut-hormone changes to the satiety and weight-loss effects of bariatric surgery — observational correlations are strong, but causal dissection is harder (Silva et al. 2012).
  • Long-term cardiovascular, pancreatic, and bone effects of chronic Y2 receptor agonism — not characterized because no PYY analogue has reached chronic licensed use.

Related peptides

  • Peptide YY (PYY, full-length) — the 36-residue precursor from which PYY(3-36) is generated by DPP-4 cleavage; the full-length PYY(1-36) has antimicrobial activity in Paneth cells that PYY(3-36) lacks
  • GLP-1(7-36) amide — the biologically active form of GLP-1, co-secreted from the same intestinal L-cells as PYY(3-36); both peptides contribute additively to postprandial satiety, and GLP-1 receptor agonists are the pharmacological success story that PYY-based drug development has not yet replicated
  • Neuropeptide Y (sheep form) — the orexigenic neuropeptide whose NPY/AgRP neurons in the arcuate nucleus are the primary synaptic target that PYY(3-36) inhibits to produce satiety
Hypotheses6 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 low levels of a natural fullness hormone after meals, in obese people, cause hunger signals in the brain to stay switched on in a way that cannot be fixed by other hormones?

If true, it would identify a specific gap in the brain's appetite control that standard obesity hormones cannot fill, potentially pointing to a treatment that works for people who do not respond to other appetite therapies.

The hypothesis
In obese individuals, the blunted postprandial PYY(3-36) release selectively impairs Y2 receptor tone in the arcuate nucleus relative to circulating NPY levels, creating a receptor occupancy imbalance that favors orexigenic over anorexigenic signaling, and this imbalance is not corrected by the compensatory hyperleptinemia of obesity.
Why it’s plausible
The literature establishes that obese subjects have blunted postprandial PYY release correlated with reduced satiety, and that the causal direction is unsettled (driver vs. consequence of obesity). Crucially, arcuate nucleus Y2 receptors serve as autoreceptors on NPY/AgRP neurons: when PYY(3-36) is low, these autoreceptors are under-occupied, disinhibiting NPY/AgRP neurons and promoting feeding. Leptin, which is elevated in obesity, also acts on POMC neurons in the arcuate but does not directly suppress NPY/AgRP output via the Y2 autoreceptor pathway. Thus the leptin resistance of obesity (documented at the receptor signaling level) would not compensate for Y2 under-occupation. This creates a specific, leptin-independent gap in appetite regulation that PYY replacement could fill even in the context of obesity's generalized hypothalamic leptin resistance.
Why it matters
If the Y2 occupancy deficit is leptin-independent, PYY(3-36) replacement would be effective precisely in the patients who are most leptin-resistant and therefore least responsive to other hypothalamic appetite interventions, defining a responder subpopulation for precision obesity medicine.
Plausibility.74
Novelty.68
Impact.73
Basis · grounding4 papers
[1]
paper
Obese individuals have lower postprandial PYY levels; the study investigated mechanisms for the observed relative PYY deficiency among obese subjects
doi: 10.1210/en.2005-0972
[2]
paper
Retained responsiveness of obese subjects to the anorectic effects of PYY3-36 supports targeting the PYY system; this responsiveness is intact even in leptin-resistant obese subjects
doi: 10.1113/jphysiol.2008.164269
[3]
paper
Anorectic efficacy of exogenous PYY3-36 is fully intact in obese persons, consistent with preserved Y2 receptor function despite other hypothalamic hormone resistance
doi: 10.1136/jcp.2007.048488
[4]
paper
Arg72 allele of peptide YY associated with increased risk of type 2 diabetes, suggesting PYY signaling interacts with metabolic pathways beyond simple appetite regulation
doi: 10.1210/en.2005-0972
openupdated 2026-06-05

Could a capsule that releases PYY(3-36) in the lower gut, the place where the body naturally makes it, reduce appetite without the nausea seen when the hormone is given through the nose?

If this delivery method works, it could offer a non-injection weight-loss treatment that avoids the nausea that derailed earlier versions of this drug, making it more tolerable than current options for people who struggle with daily injections.

The hypothesis
PYY(3-36) administered via colon-targeted oral formulation would achieve sufficient mucosal and portal absorption to suppress appetite without the acute nausea that terminated the Nastech intranasal program, because the distal gut is the site of endogenous L-cell release and exposure to a prolonged local concentration profile mimics the physiologic postprandial release kinetics.
Why it’s plausible
The Nastech intranasal Phase 2 failure was attributed to rapid systemic absorption producing peak plasma levels that exceeded the nausea threshold. The physiologic release of PYY(3-36) from L-cells in the distal ileum and colon generates a slow, sustained portal exposure profile that tracks meal duration. A pH-triggered or microbiome-triggered colon-targeted oral delivery system would place the peptide at the site of endogenous secretion, allowing gut-wall transcytosis and enteric nerve engagement before systemic exposure peaks. The oral bioavailability axis hits note that the GI tract complicates oral administration of peptides, but also that the ileal brake mechanism (inhibition of gastric emptying by the terminal ileum) is an established PYY peripheral effect that does not require CNS penetration. PYY(3-36) has a approximately 3 hour functional half-life and the reversible PEGylation data confirm that half-life extension is possible without permanent inactivation.
Why it matters
A tolerable oral or colon-targeted formulation would remove the nausea liability that killed previous programs and enable chronic obesity treatment without the injection burden that limits GLP-1 agonist adherence in some populations.
Plausibility.69
Novelty.60
Impact.74
Basis · grounding4 papers
[1]
paper
Rapid absorption and significant nausea following prandial intranasal administration of PYY3-36 to obese subjects over 12 weeks; Nastech Phase 2 failure attributed to tolerability
doi: 10.5009/gnl.2012.6.1.10
[2]
paper
PYY infusions in humans delayed gastric emptying and mouth-to-cecum transit time; ileal brake mechanism operates peripherally without CNS entry
doi: 10.1381/096089206776944959
[3]
paper
Reversible PEGylation through spontaneously cleavable linker gave 8-fold increase in functional half-life (3h to 24h), proof that half-life extension without permanent inactivation is achievable
doi: 10.1136/jcp.2007.048488
[4]
paper
Oral tablet modality may provide additional safety, cost-effectiveness, and shelf-stability benefits for peptide therapeutics despite GI tract barriers
doi: 10.1007/s13346-025-01978-7
openupdated 2026-06-05

Could giving PYY(3-36) before meals protect people who have had gastric bypass surgery from the dangerous blood-sugar crashes that can happen after eating?

Post-bypass low blood sugar affects up to 30% of gastric bypass patients and has no approved drug treatment. If this approach works, it could help a large group of patients who currently have very few options for managing this serious complication.

The hypothesis
PYY(3-36) suppresses post-bariatric hypoglycemia by acutely dampening the exaggerated postprandial GLP-1 and insulin surges that follow Roux-en-Y gastric bypass, via Y2-receptor-mediated inhibition of L-cell co-secretion feedback and slowing of gastric emptying.
Why it’s plausible
Post-bariatric hypoglycemia (PBH) is a recognized complication of Roux-en-Y bypass in which exaggerated nutrient delivery to the small bowel triggers extreme GLP-1 and insulin surges causing postprandial hypoglycemia. The readme documents that bariatric surgery produces exaggerated postprandial PYY release, and that GLP-1 and PYY are co-secreted from L-cells additively. However, there is a distinction between the acute post-meal period (when both GLP-1 and PYY are elevated) and the late postprandial phase (when PYY's sustained presence might dampen further L-cell activation via Y2 autoreceptor feedback). The Y2 receptor is expressed on intestinal L-cells as an autoreceptor that limits further PYY and GLP-1 secretion. Additionally, PYY(3-36) slows gastric emptying independently of GLP-1. In PBH patients whose endogenous PYY surge may be insufficient to counteract the GLP-1 spike, exogenous PYY(3-36) pre-dosing before meals could attenuate the GLP-1 bolus and reduce insulin overshoot.
Why it matters
Post-bariatric hypoglycemia affects 10-30% of Roux-en-Y patients and has no approved pharmacological treatment; a pre-meal PYY(3-36) strategy would repurpose an endogenous satiety peptide as an anti-hypoglycemic intervention in a high-unmet-need population.
Plausibility.62
Novelty.72
Impact.72
Basis · grounding3 papers · 1 computed/note
[1]
paper
GLP-1 and PYY are co-secreted from L-cells; additive appetite suppression in co-infusion studies; mechanistic basis for combination gut-hormone approaches
doi: 10.5009/gnl.2012.6.1.10
[2]
noteRoux-en-Y gastric bypass produces exaggerated postprandial PYY release, sustained for years, cited as contributing to durable post-surgical satiety
[3]
paper
Y1 and Y2 receptors are localized in intestinal epithelial cells and submucosal plexus, consistent with autocrine/paracrine regulation of L-cell secretion
doi: 10.1016/j.npep.2019.101973
[4]
paper
PYY infusions delayed gastric emptying and mouth-to-cecum transit, a peripheral effect that would reduce rate of nutrient delivery to L-cells post-bypass
doi: 10.1381/096089206776944959
openupdated 2026-06-05

Does this natural fullness hormone reduce the pleasure-driven urge to eat, through a different brain pathway than the one that controls basic hunger, and can those two effects be separated?

If the two effects are separable, it could open the door to treatments aimed specifically at compulsive or reward-driven eating, such as binge eating disorder, rather than just calorie-based appetite suppression.

The hypothesis
PYY(3-36) suppresses hedonic eating through Y2 receptor-mediated modulation of mesolimbic dopamine circuitry independently of its hypothalamic NPY/AgRP-POMC axis action, and these two arms of its anorectic mechanism are dissociable by dose and route of administration.
Why it’s plausible
The readme explicitly states that PYY(3-36) modulates both homeostatic and hedonic brain circuitry, and fMRI studies show hypothalamic activity shifts. The literature notes that activity shifts toward an orbitofrontal cortex pattern during IV PYY(3-36) infusion (selectivity axis chunk from 10.5009/gnl.2012.6.1.10). The mesolimbic dopamine system (VTA to nucleus accumbens) governs food reward, and Y2 receptors are expressed in the VTA. If the two arms are dissociable, it would explain why some human infusion studies show appetite reduction without proportional changes in subjective hunger ratings, and why the primate data show time-of-day specificity (morning but not evening inhibition of food intake). The C-terminal TRQRY motif of PYY(3-36) is the core Y2 pharmacophore that would engage both hypothalamic and mesolimbic Y2 sites at physiologic concentrations.
Why it matters
If the hedonic arm is separable, analogue engineering could bias toward or away from reward-circuit engagement, with implications for binge-eating disorder and food addiction indications beyond simple caloric restriction obesity.
Plausibility.67
Novelty.62
Impact.68
Basis · grounding3 papers · 1 computed/note
[1]
paper
PYY3-36 modulates both homeostatic and hedonic brain circuitry; this was cited to support ongoing obesity treatment development
doi: 10.1113/jphysiol.2008.164269
[2]
paper
fMRI showed activity shifted to OFC (orbitofrontal cortex) when PYY3-36 was infused intravenously, implicating reward circuitry
doi: 10.5009/gnl.2012.6.1.10
[3]
paper
Primate rhesus data showed inhibition of morning but not evening food intake, consistent with circuit-specific temporal modulation
doi: 10.1210/en.2005-0972
[4]
sequenceC-terminal TRQRY motif is the Y2 pharmacophore shared with NPY; Y2 receptors are expressed in VTA and nucleus accumbens in addition to the arcuate nucleus
openupdated 2026-06-05

Are the receptors currently listed as the main targets for PYY(3-36) actually wrong, the result of a data mix-up, with the real target being a different receptor entirely?

If the listed targets are corrected, researchers and anyone building tools on top of this data would avoid being misled down the wrong drug design or combination-therapy paths, saving time and resources.

The hypothesis
The annotated primary targets GLP-1R and NPBWR1 are incorrect for PYY(3-36); the true primary target is the Y2 receptor (NPY2R), and the card's target annotation reflects database cross-contamination rather than experimentally validated binding.
Why it’s plausible
All literature evidence in the bundle consistently identifies the Y2 receptor as the receptor through which PYY(3-36) produces its anorectic effect: the Y2 knockout abolishes the anorectic response in rodents, the mechanism is described as Y2 autoreceptor-mediated suppression of NPY/AgRP neurons, and selectivity chunks explicitly state that the N-terminal truncation from PYY(1-36) to PYY(3-36) confers Y2 selectivity by removing the N-terminal dipeptide required for Y1/Y4/Y5 recognition. The reference chunks about GLP-1R and NPBWR1 discuss those receptor systems entirely in isolation from PYY binding data. The boltz-2 complex prediction has a high iptm of 0.94, which if modelled against GLP-1R or NPBWR1 would be hard to reconcile with the absence of any published PYY(3-36) binding data at those receptors; the high interface confidence is more consistent with a Y2 complex.
Why it matters
Correcting the target annotation from GLP-1R/NPBWR1 to Y2R removes a misleading framework that would misdirect structure-activity, pharmacology, and combination-therapy reasoning for every downstream use of this card.
Plausibility.94
Novelty.18
Impact.85
Basis · grounding3 papers · 1 computed/note
[1]
paper
PYY3-36 is a selective, high-affinity agonist of Y2 receptors; PYY1-36 binds all four Y receptor subtypes but the N-terminal truncation confers Y2 selectivity
doi: 10.1007/s00125-014-3292-y
[2]
paper
Anorectic efficacy attributed to activating autoinhibitory Y2-R on NPY/AgRP neurons; Y2R knockout abolishes effect
doi: 10.1136/jcp.2007.048488
[3]
paper
Y2-receptor binds only the C-terminal of PYY; deletion of N-terminal tyrosineproline of PYY(1-36) prevents Y1/Y4/Y5 binding, yielding Y2-selective PYY(3-36)
doi: 10.1381/096089206776944959
[4]
structureComplex prediction iptm=0.94 is high; if modelled against GLP-1R it would require documented binding evidence that is absent from the entire literature bundle
openupdated 2026-06-05

Does a particular coiled section in the middle of the PYY(3-36) molecule make direct contact with its target receptor, and would breaking that coil destroy the hormone's ability to bind?

If this structural detail is confirmed, it could guide scientists to design smaller, more stable versions of the hormone that keep the appetite-suppressing effect but are easier to manufacture and less prone to breakdown in the body.

The hypothesis
The RYYASLR motif at positions 8-14 of PYY(3-36) (corresponding to residues 10-16 of full-length PYY) forms an amphipathic alpha-helix that makes direct contact with the extracellular loop 2 of the Y2 receptor, and disruption of this helix by proline substitution at Y10 or A13 abrogates Y2 binding without affecting the C-terminal RQRYamide pharmacophore.
Why it’s plausible
The Y2 receptor binds only the C-terminal of NPY family peptides, and PYY(3-36) has a 34-residue sequence with the C-terminal QRPY (reading from the C-terminus as Yam-RQR) being essential for receptor contact. However, solution NMR studies of NPY and PYY have consistently shown a central amphipathic helix in the mid-region of these peptides. In PYY(3-36), the sequence RYYASLRHYLNLVTR (residues 8-22 of the 34-mer) contains a pattern of hydrophobic residues (Y, L, Y, L, L, V) and polar/charged residues (R, A, S, R, H, N, T) consistent with amphipathic helix formation on a helical wheel. The structural prediction reports avg_plddt of 71.9, which is moderate confidence suggesting partial disorder, consistent with the known PP-fold conformation of PYY in which the polyproline-II N-terminal arm and the C-terminal helix are connected by a turn. The helix is likely critical for receptor engagement because a hairpin-loop rather than an extended chain would position the C-terminus optimally for the Y2 binding pocket.
Why it matters
Identifying the helical segment's role in Y2 engagement would guide truncation and cyclization strategies to design minimal Y2 agonists with improved proteolytic stability while preserving the anorectic pharmacophore.
Plausibility.34
Novelty.52
Impact.58
Basis · grounding2 papers · 2 computed/notes
[1]
sequenceResidues 8-22 RYYASLRHYLNLVTR contain alternating hydrophobic (Y9, Y10, L13, H15, L16, L18, V19) and polar/charged (R8, A11, S12, R14, N17, T20) residues consistent with amphipathic alpha-helix pattern
[2]
structureavg_plddt=71.9 indicates partial disorder; complex iptm=0.94 indicates confident interface prediction; moderate plddt is consistent with the known PP-fold where only the helical arm is ordered
[3]
paper
Y2-receptor binds only the C-terminal; however the intact mid-region helix is needed to orient the C-terminal pharmacophore relative to the receptor binding pocket
doi: 10.1381/096089206776944959
[4]
paper
PYY3-36 is a selective, high-affinity Y2 agonist; selectivity is due to the N-terminal truncation, implying the remaining structure including the helix is permissive for Y2 but not Y1/Y4/Y5 binding
doi: 10.1007/s00125-014-3292-y
details expand to inspect
full evidence table2 metrics
metricvaluetool
ipTM 0.9421985149383545 boltz-2
ranking score 0.7633717060089111 boltz-2
3-letter notation
Ile-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 strategycolabfold_nvidia
diffusion samples1
runtime
predicted bymlx@peptide
predicted at2026-04-25
citationbibtex
peptidemodel (2026). PYY(3-36): natural fullness hormone released after eating (pep-10604, v1). PeptideModel. https://peptidemodel.com/card/pep-10604
@peptide{pep10604,
  sequence = {IKPEAPGEDASPEELNRYYASLRHYLNLVTRQRY},
  target   = {npy2r},
  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 12 papers
[3] supporting
[5] supporting
[12]
The satiety hormone peptide YY as a regulator of appetite
Vincent, R. et al. Journal of Clinical Pathology 2008
supporting
discussion no comments
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peptidemodel.com CC-BY-SA-4.0 research only · not for human use