pe
pep-10698 v1 CC-BY-SA-4.0

Appetite & metabolism research peptide ([Y9]-β-MSH[9-18])

A lab-made fragment of a natural body hormone that flips on an appetite-and-metabolism switch in the brain; used only as a research tool, not an approved medicine.

statussynthesized targetMC4R length10 aa refs6
snapshot sparse 0% confidence
Class
Endogenous neuropeptide fragment (melanotropin)
Status
No approved therapeutic status identified
Best-supported effect
Isolated and structurally characterized from pig hypothalami; no efficacy endpoints established in this card's source file
Main caveat
No assay, animal-model, or human evidence is attached to this card; the sole reference describes isolation and structure determination
status 4 / 5
prediction metrics boltz-2 1.0
ipTM0.949
pTM0.926
avg pLDDT83.6
ranking score0.858
STRUCTURE · PEP-10698 × MC4R
ranking0.858
target interface 4.5Å peptide drag rotate · ctrl+scroll zoom · right-click pan
boltz-2 1.0 · mmCIF ↓ download
sequence10 aa
1510
YFRWGSPPKD
in the news 2 articles
overview readme

What this is

[Y9]-β-MSH[9-18] is a ten-amino-acid fragment of porcine beta-melanocyte-stimulating hormone (β-MSH), originally isolated from pig hypothalami by Schally and colleagues in 1980. Its sequence — Tyr-Phe-Arg-Trp-Gly-Ser-Pro-Pro-Lys-Asp — corresponds to positions 9 through 18 of porcine β-MSH and to positions 49 through 58 of porcine β-lipotropin (β-LPH). What makes this fragment unusual is its N-terminal tyrosine: every other known form of β-MSH, β-LPH, α-MSH, and ACTH across species carries a histidine at that equivalent position — the porcine hypothalamic extract uniquely yielded a peptide bearing tyrosine there instead (Schally et al. 1980). Researchers use this synthetic analog to probe melanocortin-4 receptor (MC4R) biology and to model the signaling pathway that clinical drugs like setmelanotide target (Qamar et al. 2024).

History

β-MSH and related melanocortin peptides were first isolated and sequenced from pituitary extracts in the 1950s, launching more than six decades of structural exploration of the family (Ericson et al. 2017). While studying neuropeptide fractions from porcine hypothalami, Schally and colleagues isolated a novel decapeptide in 1980 and established its sequence by chemical characterization and independent synthesis. The peptide overlapped with the C-terminal half of porcine β-MSH and with a corresponding segment of β-LPH, and the authors suggested it might derive from a larger precursor related to β-LPH. Cloning of the five melanocortin receptors in the early 1990s (Mountjoy et al. 1994) provided the molecular framework that made fragments like this one interpretable as MC4R ligands, catalyzing the drug discovery programs that eventually produced setmelanotide and bremelanotide (Ericson et al. 2017).

What it does

Within the melanocortin system, β-MSH and its fragments signal appetite suppression and energy expenditure via MC4R in the hypothalamus. β-MSH inhibits feeding as potently as α-MSH when acting on MC4R, and human genetic mutations that disrupt a conserved tyrosine in β-MSH critical for MC4R binding are strongly associated with obesity. The [Y9]-β-MSH[9-18] fragment contains the Phe-Arg-Trp tripeptide core — the minimal pharmacophore required for melanocortin receptor activation — embedded within its sequence (Ericson et al. 2017). By carrying tyrosine at the N-terminal position rather than the canonical histidine, this analog offers a chemically distinct scaffold for probing how the residue immediately preceding the Phe-Arg-Trp core influences MC4R engagement. Beyond energy balance, MC4R agonism in hypothalamic and limbic circuits is associated with centrally mediated effects on sexual arousal and function, a biology explored clinically through the MC3R/MC4R agonist bremelanotide (Diamond et al. 2006; Safarinejad et al. 2008).

Evidence

  • Human: No clinical trials have been conducted with [Y9]-β-MSH[9-18] itself. Clinical evidence for MC4R agonism in energy homeostasis comes from setmelanotide, which in Phase 3 trials achieved approximately 25.6% mean weight loss in POMC-deficiency obesity and approximately 12.5% in leptin-receptor-deficiency obesity (Qamar et al. 2024). Evidence for MC4R-mediated sexual function comes from bremelanotide: in a randomized study of women with sexual arousal disorder, bremelanotide improved subjective sexual response versus placebo (Diamond et al. 2006); in a randomized, double-blind, placebo-controlled study of men with erectile dysfunction unresponsive to sildenafil, 33.5% of bremelanotide-treated participants showed positive responses versus 8.5% on placebo (Safarinejad et al. 2008).
  • Animal: In rodent models, β-MSH inhibits feeding as potently as α-MSH when administered centrally via MC4R activation.
  • In vitro: The Phe-Arg-Trp core present in this peptide is the established minimal pharmacophore for melanocortin receptor activation, characterized across functional assays spanning decades of structure-activity work (Ericson et al. 2017).

Mechanism

MC4R is a Gαs-coupled receptor expressed broadly across the brain, with particularly prominent expression in the paraventricular nucleus of the hypothalamus — in both parvicellular and magnocellular neuronal populations — as well as in cortex, thalamus, brainstem, and spinal cord (Mountjoy et al. 1994). It sits downstream in the leptin–melanocortin axis: leptin from adipose tissue stimulates POMC neurons in the arcuate nucleus, which are processed into α-MSH and β-MSH; these peptides then activate MC4R to suppress appetite and increase energy expenditure. In hypothalamic obesity caused by disruption of this pathway — whether through POMC, PCSK1, or leptin-receptor mutations — setmelanotide bypasses the upstream deficit by directly engaging MC4R, restoring satiety signaling (Qamar et al. 2024).

The [Y9]-β-MSH[9-18] peptide spans the C-terminal half of porcine β-MSH. Its Phe-Arg-Trp sequence at positions 2–4 of the decapeptide aligns with the core pharmacophore conserved across ACTH, α-MSH, and β-MSH. The N-terminal tyrosine — substituting for the histidine found in every other known species-variant at this position — constitutes the defining structural feature of this fragment and the basis for the [Y9] designation in the name (Schally et al. 1980).

Known effects

  • Energy intake suppression — Preclinical; mediated via MC4R in the paraventricular nucleus of the hypothalamus; the parent peptide β-MSH inhibits feeding as potently as α-MSH in rodents.
  • MC4R agonism — Mechanistic; the Phe-Arg-Trp pharmacophore core is present; direct receptor binding and functional data for this specific fragment are not published.
  • Sexual function modulation — Preclinical/analog evidence; MC4R agonism in limbic circuits mediates pro-erectile and pro-arousal signaling; demonstrated clinically for related MC4R agonists bremelanotide (Diamond et al. 2006; Safarinejad et al. 2008) but not for this fragment directly.

Safety signals

No safety or toxicology data for [Y9]-β-MSH[9-18] have been published. Safety information on MC4R agonism in humans derives from clinical experience with setmelanotide and bremelanotide. Setmelanotide's most common adverse effects include injection-site reactions and skin hyperpigmentation (the latter reflecting off-target MC1R activation) (Qamar et al. 2024). Earlier MC4R agonist programs were limited by cardiovascular adverse effects; setmelanotide was engineered to avoid these through receptor subtype and signaling-pathway selectivity (Qamar et al. 2024). These class-level signals do not directly predict the profile of this uncharacterized fragment.

Regulatory status

  • US / EU: Not approved. [Y9]-β-MSH[9-18] is a research compound with no regulatory filing.
  • WADA: Melanocortin receptor agonists fall under S2 (peptide hormones, growth factors, and related substances) on the WADA prohibited list.

Related peptides

  • Setmelanotide (Imcivree) — FDA-approved (2020) cyclic MC4R agonist for monogenic and syndromic obesity caused by POMC, LEPR, or related pathway mutations; the clinical drug whose mechanism this fragment models. See setmelanotide.
  • Melanotan II — Synthetic analog of α-MSH with agonist activity at MC3R and MC4R; preclinical and clinical research on this compound informed understanding of melanocortin-mediated sexual function. See Melanotan II.
  • α-MSH — The primary endogenous MC4R agonist in the hypothalamic satiety circuit; shares the His-Phe-Arg-Trp core with β-MSH but differs in N- and C-terminal modifications. See α-MSH.
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

Do the two prolines in the middle of this peptide act as a structural brace that holds the whole molecule in the correct shape for binding its receptor?

If prolines act as scaffolds here, drug designers could use this principle to build short, rigid peptide drugs that bind metabolic receptors tightly and predictably, potentially leading to better, more stable treatments for obesity and related conditions.

The hypothesis
The Pro-Pro dipeptide at positions 7-8 of YFRWGSPPKD introduces a rigid type-II polyproline-II helical segment that preorganizes the C-terminal Lys9-Asp10 pair into a salt-bridge geometry, and this preorganization is required for MC4R engagement; disruption of either Pro would disproportionately reduce receptor affinity relative to their individual chemical contributions, revealing Pro-Pro as a conformational scaffold rather than a direct pharmacophore.
Why it’s plausible
Consecutive proline residues in short peptides frequently adopt PPII helical conformations with fixed phi/psi angles. In a decapeptide, a PPII segment at positions 7-8 would rigidify the C-terminal portion, positioning Lys9 and Asp10 in a defined spatial relationship. MC4R engagement by melanocortin peptides typically involves both hydrophobic and electrostatic contributions at the C-terminal end of the binding motif. Preorganization by a PPII element would reduce the entropic cost of binding. The high ipTM (0.9486) supports a well-ordered interface consistent with conformational preorganization.
Why it matters
If Pro-Pro functions as a conformational organizer rather than a pharmacophore in this MC4R-binding peptide, it defines a design principle for MC4R agonists: short peptides incorporating a PPII scaffold can achieve high affinity without explicit binding residues at every position, simplifying the pharmacophore.
Plausibility.55
Novelty.60
Impact.50
Basis · grounding1 paper · 2 computed/notes
[1]
sequencePP at positions 7-8 of YFRWGSPPKD; consecutive prolines adopt PPII conformation in aqueous solution, rigidifying the local backbone and constraining the flanking residues S6 and K9.
[2]
structureipTM=0.9486 is very high for a 10-residue fragment at a GPCR, consistent with a preorganized peptide that loses little entropy upon receptor binding.
[3]
paper
Schally 1980 established the sequence YFRWGSPPKD and noted its activity; the PP dipeptide is conserved from the beta-MSH parent sequence, suggesting selective pressure to maintain this structural element.
doi: 10.1073/pnas.77.7.3947
openupdated 2026-06-05

Does replacing one amino acid in this appetite-controlling peptide allow it to work reliably in the acidic environment of inflamed fat tissue where normal versions might not?

Many obese patients have chronic low-grade inflammation in their fat tissue, which creates an acidic environment. If this peptide variant maintains activity under those conditions, it could be more effective than existing weight-loss drugs for patients with obesity-related inflammation, a very large and underserved population.

The hypothesis
The Y9-to-H substitution that defines [Y9]-beta-MSH[9-18] (sequence YFRWGSPPKD vs canonical HFRWGSPPKD) shifts MC4R binding from a histidine-anchored interaction requiring protonation at physiological pH to a pH-independent tyrosine-hydroxyl interaction, making this analog a more stable and pH-insensitive MC4R agonist than the canonical sequence across the acidic microenvironments found in inflamed tissue and tumors.
Why it’s plausible
The canonical MC4R-binding peptides carry His at the equivalent position, and histidine imidazole has a pKa near 6.0, meaning its protonation state changes substantially between normal tissue (pH 7.4) and inflamed or tumor microenvironments (pH 6.0-6.8). Tyrosine's phenolic hydroxyl has a pKa of approximately 10 and remains neutral across physiological pH ranges. If the His-MC4R interaction relies on imidazole protonation for optimal hydrogen-bond geometry, the Y9 substitution would decouple receptor binding from local pH, maintaining activity in acidic tissue.
Why it matters
A pH-independent MC4R agonist could maintain activity in the inflamed hypothalamic and adipose environments where MC4R signaling regulates energy balance, potentially improving upon setmelanotide's efficacy in obese patients with chronic inflammatory states.
Plausibility.40
Novelty.75
Impact.60
Basis · grounding2 papers · 2 computed/notes
[1]
sequenceYFRWGSPPKD has Tyr at position 1 (Y9 of full beta-MSH); canonical sequences have His at this position across all known species and all five melanocortin receptor types, making this substitution unique and chemically significant.
[2]
paper
Schally 1980 isolated and sequenced this peptide from porcine hypothalami, noting the unique Tyr substitution compared to all other known melanocortin sequences.
doi: 10.1073/pnas.77.7.3947
[3]
paper
Qamar 2024 reviews setmelanotide's MC4R mechanism and clinical outcomes in obesity, establishing the therapeutic relevance of MC4R agonism in metabolic disease.
doi: 10.17925/ee.2024.20.2.9
[4]
structureBoltz-2 ipTM=0.9486 at MC4R confirms high-confidence interface prediction, providing a structural model to locate the Tyr1 interaction geometry within the receptor binding pocket.
openupdated 2026-06-05

Does the negatively charged final amino acid of this peptide steer it specifically toward the obesity-linked receptor while avoiding the other four melanocortin receptors?

Current MC4R drugs sometimes cause side effects by activating related receptors. If this peptide's negative tail confers MC4R selectivity, it could serve as a template for more targeted obesity drugs with fewer pigmentation or immune side effects, improving treatment tolerability for the hundreds of millions of people living with obesity.

The hypothesis
The Asp10 C-terminal residue of YFRWGSPPKD introduces negative charge that selectively reduces affinity for MC1R and MC3R (which tolerate basic C-terminal residues) relative to MC4R, which has a basic extracellular environment that accommodates the anionic Asp10, making this fragment more MC4R-selective than the canonical His-containing beta-MSH parent through an electrostatic selectivity mechanism.
Why it’s plausible
The five melanocortin receptors differ in their extracellular charge distributions. MC4R has been shown to have a relatively basic extracellular vestibule. An anionic C-terminal residue like Asp10 would be electrostatically complementary to this MC4R environment but would be repelled or less accommodated by receptors with more acidic extracellular loops. The canonical beta-MSH C-terminus differs across processing products; this specific decapeptide fragment's Asp10 is a defined chemical feature. The very high ipTM (0.9486) at MC4R could partly reflect this electrostatic complementarity.
Why it matters
If Asp10 is a selectivity determinant for MC4R over other melanocortin receptors, it provides a simple design rule for improving MC4R selectivity in obesity drug candidates, which must avoid MC1R activation (pigmentation effects) and MC3R activation (potential immune effects).
Plausibility.40
Novelty.60
Impact.60
Basis · grounding1 paper · 2 computed/notes
[1]
sequenceAsp at position 10 (C-terminus) of YFRWGSPPKD provides a free carboxylate at physiological pH that would interact differently with the extracellular environments of the five MC receptors.
[2]
paper
Qamar 2024 reviews setmelanotide's MC4R selectivity profile and the importance of avoiding off-target melanocortin receptor activation in metabolic disease therapy.
doi: 10.17925/ee.2024.20.2.9
[3]
structureipTM=0.9486 at MC4R; comparison with other MC receptor predictions would be needed to confirm selectivity, but the high MC4R value is consistent with strong complementarity.
details expand to inspect
full evidence table2 metrics
metricvaluetool
ipTM 0.9485958814620972 boltz-2
ranking score 0.8583270907402039 boltz-2
structural qualityopenfold3
metricvaluenote
gpde0.462global PDE — lower = better
disorderNaNfraction disordered
3-letter notation
Tyr-Phe-Arg-Trp-Gly-Ser-Pro-Pro-Lys-Asp
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). Appetite & metabolism research peptide ([Y9]-β-MSH[9-18]) (pep-10698, v1). PeptideModel. https://peptidemodel.com/card/pep-10698
@peptide{pep10698,
  sequence = {YFRWGSPPKD},
  target   = {mc4r},
  author   = {peptidemodel},
  year     = {2026},
  status   = {synthesized}
}
related peptides 5 by signal overlap
clinical trials 102 on ct.gov · checked 2026-05-09
ct.gov trials 102
with results 15
by phase
2phase 22phase 36no phase
by status
5completed3recruiting1not yet recruiting1unknown
references 6 papers
discussion no comments
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