pe
pep-10561 v1 CC-BY-SA-4.0

Kisspeptin-54: natural hormone that triggers puberty and fertility signaling

A natural brain hormone that tells the body to start and maintain puberty and reproductive cycles; studied as a potential fertility treatment but not yet an approved drug.

statussynthesized targetKISS1R length54 aa refs69
status 4 / 5
prediction metrics boltz-2 2.2.1
ipTM0.890
pTM0.837
avg pLDDT63.4
ranking score0.685
STRUCTURE · PEP-10561 × KISS1R
ranking0.685
target interface 4.5Å peptide drag rotate · ctrl+scroll zoom · right-click pan
boltz-2 2.2.1 · mmCIF ↓ download
sequence54 aa
1510152025303540455054
GTSLSPPPESSGSRQQPG LSAPHSRQIPAPQGAVLV QREKDLPNYNWNSFGLRF
overview readme

Snapshot

Aliases: Metastin (human)
Class: Endogenous neuropeptide / KISS1R ligand
Evidence tier: In vitro / assay evidence
Status: No approved therapeutic status identified in attached sources
Best-supported effect: High-affinity binding to kisspeptin receptor (KISS1R / GPR54) in receptor-binding assays (Ki ~1.45 nM at human GPR54, ~1.81 nM at rat GPR54)
Main caveat: Receptor-binding data do not establish in vivo efficacy; no animal efficacy data or human trial data are identified


What this is

Kisspeptin-54 (KP54) is the full-length, 54-amino-acid human form of kisspeptin, an endogenous peptide encoded by the KISS1 gene. It is also known under the historical alias Metastin, which reflects its initial identification as a product of a metastasis-suppressor gene locus. KP54 is the endogenous ligand for the G-protein-coupled receptor KISS1R (GPR54), a receptor involved in reproductive neuroendocrine regulation and, based on the gene's original characterization, in the suppression of tumor metastasis. The 54-residue sequence includes the conserved C-terminal RF-amide motif shared with shorter kisspeptin fragments (KP10, KP13, KP14), which are considered the minimally active receptor-binding region.


Evidence map

Evidence layerGradeWhat it supports
HumanNone identifiedNo human trial data identifieds available literature
AnimalNone identifiedReferenced animal study (mouse gonadotropin; Gottsch 2004) listed in source but animal efficacy data not individually extracted
In vitroIn vitro moderateReceptor-binding assay data: Ki 1.81 nM (rat GPR54) and 1.45 nM (human GPR54); source also describes KISS1-encoding-gene role in tumor-metastasis suppression and gonadotropin stimulation
ComputationalNone identifiedNo computational or structural prediction data attached
MechanismPlausibleAgonism at KISS1R (GPR54) is the stated primary mechanism; downstream gonadotropin-releasing hormone (GnRH) pathway engagement is biologically plausible based on the receptor class

Claim check

ClaimVerdictEvidence layerConfidence
Binds KISS1R (GPR54) with high affinitySupported (in vitro)In vitroMedium — Ki values from single vendor-source catalog entry; independent replication not extracted
Stimulates gonadotropin secretionSupported (in vitro / early animal)In vitroLow — stated as catalog descriptor with supporting reference (mouse model, Gottsch 2004); detailed study data not individually extracted
Suppresses tumor metastasisWeak (in vitro / descriptor)In vitroLow — stated as catalog descriptor based on the KISS1 gene's metastasis-suppressor characterization (Kotani 2001); no in vivo anti-metastatic trial data attached
Human therapeutic use for any indicationNot establishedNoneHigh — no human trial data present

Assay conditions

This section reports concentrations or conditions used in assays. It does not establish animal or human exposure.

ContextSystemAssay conditionTimepointEndpointLimitation
Receptor-binding assayRat GPR54 receptorConcentration yielding Ki = 1.81 nMNot individually extractedReceptor binding affinity (Ki)Single catalog-available data point; assay protocol not fully described in source
Receptor-binding assayHuman GPR54 receptorConcentration yielding Ki = 1.45 nMNot individually extractedReceptor binding affinity (Ki)Single catalog-available data point; assay protocol not fully described in source

Assay limitations

  • Binding Ki values are reported as catalog descriptor data; the original assay methodology, conditions, and controls are not individually extracted's available literature.
  • Receptor binding affinity does not establish functional agonism, downstream signaling magnitude, or in vivo activity.
  • No animal efficacy data or human safety or efficacy data are identified.
  • In vitro binding data cannot be extrapolated to systemic pharmacokinetics, bioavailability, or therapeutic outcome in any species.

Regulatory status

No approved therapeutic status identified. This card describes a research-grade peptide based on an endogenous human sequence. No FDA, EMA, or equivalent major regulatory approval for any therapeutic use is described in the attached sources.

Region / bodyStatusNotes
US (FDA)No approved therapeutic use identifiedNot an approved drug; research-grade synthetic peptide
EU (EMA)No approved therapeutic use identifiedStatus not extracted in source
WADANot checked in this cardSource-bundle does not address anti-doping classification

Mechanism

KP54 is an agonist at KISS1R (GPR54), a Gq/11-coupled G-protein-coupled receptor. Receptor activation engages phospholipase C–mediated signaling, increasing intracellular calcium. In the hypothalamic reproductive axis, KISS1R activation on GnRH neurons is recognized as a key upstream regulator of GnRH pulse generation and gonadotropin (LH, FSH) release. The connection to tumor-metastasis suppression reflects the original KISS1 gene characterization: the gene product was identified as a suppressor of metastatic colonization, independent of primary tumor growth. The specific mechanism by which KP54 or its fragments inhibit metastatic signaling is not fully described in the attached source.

The receptor target (KISS1R / GPR54) is stated consistently in available literature. Binding data (Ki values) are from in vitro assay; downstream functional activity in human tissue is not characterized in the attached source.


Chemistry

FieldValue
Sequence (one-letter)GTSLSPPPESSGSRQQPGLSAPHSRQIPAPQGAVLVQREKDLPNYNWNSFGLRF-NH2
Length54 amino acids
C-terminal modificationC-terminal amidation (-NH2)
TopologyLinear
N-terminusFree (H-)
Molecular weightNot provided in source
FormulaNot provided in source
CASNot provided in source
Sequence confidenceNeeds review — single vendor-source; not cross-checked against an independent primary sequence database in this card

The sequence contains the conserved C-terminal RF-amide motif (…SFGLRF-NH2), shared with the shorter kisspeptin fragments (KP10, KP13, KP14) and considered the minimally active KISS1R-binding region.


Open questions

  • In vivo efficacy — reproductive axis: Does exogenous administration of KP54 produce a reproducible, dose-dependent gonadotropin response in human subjects? Animal and clinical data for shorter kisspeptin fragments exist in the broader literature but are not extracted's available literature.
  • Anti-metastatic mechanism: What specific receptor pathway mediates KISS1-associated metastasis suppression? the gene's metastasis-suppressor role but does not detail the molecular mechanism attached to KP54 specifically.
  • Fragment vs full-length activity: Shorter kisspeptin fragments (KP10) are widely studied for KISS1R agonism; whether KP54 confers distinct pharmacological properties relative to KP10 in vivo is not addressed in the attached source.
  • Human safety profile: No toxicology, pharmacokinetics, or adverse-event data for exogenous KP54 administration are identified.
  • Formulation and stability: lyophilized storage at ≤ −20 °C; in vivo formulation, stability, and route-specific pharmacokinetics are not addressed.
Hypotheses5 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

Does the extra, probably unstructured section of KP54 change how strongly and how long it activates its receptor compared to shorter kisspeptin fragments?

If true, doctors could pick a longer-acting or shorter-acting kisspeptin form for fertility treatment, better matching natural hormone pulses. The idea is reasonable but not yet shown: real differences between KP54 and the shorter KP10 are reported in animals, while the specific structure numbers behind this proposal are not in this card.

The hypothesis
The proline-rich N-terminal extension of KP54 (roughly residues 1-44, containing multiple P-P and SPPP motifs) does not fold upon KISS1R binding but instead acts as a steric spacer that controls receptor residence time and biased agonism relative to shorter kisspeptin fragments (KP10/KP13), making KP54 a functionally distinct, not merely longer, agonist.
Why it’s plausible
The pLDDT of 63.4 against a high-confidence complex (ipTM 0.89) implies the N-terminal region remains disordered even in the bound state. The sequence GTSLSPPPESSGSRQQPGLSAPHSRQIPAPQGAVLVQREK contains six prolines clustered in SPPP and QIPAPQ tracts, which resist helical or beta-strand formation. Disordered tails on GPCRs can slow receptor internalization or modulate G-protein vs. beta-arrestin coupling.
Why it matters
If the N-terminal disorder tail biases KP54 signaling away from receptor internalization, it explains why KP54 has different in vivo potency and duration than KP10 despite identical RF-amide pharmacophore, and would guide which fragment to develop for sustained vs. pulsatile GnRH stimulation.
Plausibility.70
Novelty.65
Impact.70
Basis · grounding2 computed/notes
[1]
structurepLDDT=63.4 combined with ipTM=0.89 indicates the complex interface is confident but the overall chain is disordered, consistent with a folded C-terminal pharmacophore and an unstructured N-terminal tail.
[2]
sequenceSequence GTSLSPPPESSGSRQQPGLSAPHSRQIPAPQGAVLVQREKDLPNYNWNSFGLRF contains SPPP, QIPAPQ, and APQG motifs (6 prolines in first 44 residues) typical of intrinsically disordered regions.
openupdated 2026-06-11

Could acting on the kisspeptin receptor, which is overactive in papillary thyroid cancer, slow tumor growth?

The receptor really is overexpressed and does fire off a growth signal in these tumor cells. But whether switching it on slows growth or speeds it up is still unknown, so it is not yet clear whether a KP54-like activator or a blocker would help. Resolving this could open a targeted option beyond surgery and radioiodine.

The hypothesis
KP54 activates KISS1R-driven MAP kinase signaling in KISS1R-overexpressing papillary thyroid cancer cells at subnanomolar concentrations, suggesting that KP54-based agonists or KISS1R antagonists could suppress proliferation in a defined molecular subtype of thyroid cancer.
Why it’s plausible
The literature directly documents KISS1R overexpression in papillary thyroid cancer and MAP kinase activation by metastin in those cells (DOI 10.1210/jcem.87.5.8626). KP54 binds KISS1R at Ki ~1.45 nM, well within a pharmacologically actionable range. Whether sustained KISS1R-MAP kinase signaling is pro- or anti-proliferative in thyroid cancer is context-dependent and not resolved by the binding data alone.
Why it matters
Papillary thyroid cancer is the most common thyroid malignancy; identifying a receptor that is overexpressed and functionally coupled to MAPK in tumor cells opens a targeted therapy avenue. Clarifying whether agonism suppresses or drives proliferation determines whether KP54 itself or a blocker is the therapeutic lead.
Plausibility.85
Novelty.45
Impact.65
Basis · grounding1 paper · 1 computed/note
[1]
paper
KISS1R overexpressed in papillary thyroid cancer and activates MAP kinase in thyroid cancer cells.
doi: 10.1210/jcem.87.5.8626
[2]
noteKi ~1.45 nM at human GPR54 confirms KP54 can engage the receptor at concentrations achievable in therapeutic dosing.
openupdated 2026-06-11

Can KP54 help stop cancer cells from spreading even in tumors that lack the kisspeptin receptor?

Some studies do show the KISS1 gene suppresses spread in cells that lack its receptor, so a receptor-free route is plausible. The specific idea here, that KP54's proline-rich region grips the surrounding tissue scaffold, is one untested guess among several. If a receptor-free route exists, it could widen which cancers might benefit.

The hypothesis
The KISS1 gene was identified as a metastasis suppressor in melanoma and breast cancer; KP54 may retain direct anti-metastatic activity in KISS1R-negative cancers through a receptor-independent mechanism involving the N-terminal proline-rich region interacting with extracellular matrix components or cell-surface heparan sulfate proteoglycans.
Why it’s plausible
The alias Metastin and DOI 10.1006/bbrc.2001.5470 reference cell growth inhibition assays predating the KISS1R identification. If anti-metastatic activity required only KISS1R, KISS1R-negative tumors would be insensitive, yet some KISS1 re-expression studies show suppression in KISS1R-low contexts. The SPPP-rich N-terminal region structurally resembles heparin-binding or matrix-interacting proline-rich sequences.
Why it matters
If KP54 suppresses metastasis via an extracellular matrix mechanism independent of KISS1R, it broadens the cancer types that could benefit and decouples anti-metastatic development from the reproductive side effects of KISS1R agonism.
Plausibility.55
Novelty.60
Impact.60
Basis · grounding1 paper · 1 computed/note
[1]
paper
Early paper on cell growth inhibition assay in the context of metastin/KISS1 as a metastasis suppressor, predating confirmation that all activity is KISS1R-mediated.
doi: 10.1006/bbrc.2001.5470
[2]
sequenceN-terminal GTSLSPPPESSGSRQQPGLSAPH region contains SPPP and serine-glycine motifs reminiscent of heparan sulfate binding and extracellular matrix-interacting proline-rich stretches.
openupdated 2026-06-11

Could engineers build a better version by replacing the part of KP54 that breaks down quickly with something that survives longer in the bloodstream?

A longer-lasting kisspeptin could mean fewer injections during fertility treatment. One caution: in animals the full-length KP54 already lasts longer than the short fragment, so the tail may matter for that staying power. Whether an engineered version truly beats native KP54 would have to be tested, not assumed.

The hypothesis
Replacing the disordered N-terminal proline-rich region of KP54 (residues 1-44) with a serum half-life-extending moiety (such as a fatty acid chain or albumin-binding peptide) while retaining the KP10 pharmacophore would yield a synthetic kisspeptin analog with enhanced metabolic stability and comparable KISS1R potency, outperforming native KP54 as a clinical candidate for hypogonadotropic hypogonadism.
Why it’s plausible
Native KP54 is rapidly degraded in vivo; its N-terminal extension contributes bulk but not structured binding energy (pLDDT 63.4, disordered proline tracts). Engineering precedents for GLP-1 and other disordered peptide hormones show that replacing disordered regions with half-life extenders preserves receptor affinity while dramatically increasing plasma persistence.
Why it matters
A long-acting KP54 analog would allow less frequent dosing in fertility treatment protocols, reducing patient burden and enabling sustained GnRH pulsatility restoration that matches physiological requirements better than short-acting KP10 peptides.
Plausibility.60
Novelty.50
Impact.60
Basis · grounding2 computed/notes
[1]
structureipTM=0.89 indicates the C-terminal pharmacophore drives the high-confidence interface; pLDDT=63.4 indicates the N-terminal region contributes disorder not structured binding contacts.
[2]
sequenceResidues 1-44 contain SPPP, QIPAPQ proline-rich tracts: classic markers of regions with no fixed secondary structure that could be replaced without losing receptor affinity.
openupdated 2026-06-11

Does KP54 send a somewhat different internal signal than KP10, even though both bind the same receptor?

If the two forms favor different internal pathways, clinicians could pick the form that avoids receptor burnout during fertility treatment. This is a reasonable but unproven idea: reported KP54-versus-KP10 differences exist, yet some studies show KP54 still drives the receptor uptake this proposal assumes it avoids, and the structure numbers cited for it are not in this card.

The hypothesis
KP54 activates KISS1R to trigger LH/FSH secretion not only through Gq-calcium signaling but also through beta-arrestin-mediated ERK1/2 activation; the 44-residue N-terminal disordered tail biases this balance toward G-protein coupling, making KP54 a G-protein-biased agonist compared to KP10 at the same receptor.
Why it’s plausible
The high ipTM (0.89) confirms a stable KP54-KISS1R complex, yet pLDDT (63.4) suggests a large disordered segment remains external. Disordered extensions on peptide agonists are known to impede receptor-beta-arrestin complex formation by reducing steric compatibility with the arrestin docking interface on the intracellular receptor surface. Biased agonism at KISS1R has not been directly tested for different-length kisspeptin forms.
Why it matters
If KP54 is G-protein-biased relative to KP10, it would cause less receptor desensitization and produce more sustained gonadotropin release, explaining discordant pharmacodynamic data between KP54 and KP10 infusion studies in clinical settings.
Plausibility.55
Novelty.55
Impact.60
Basis · grounding2 computed/notes
[1]
structureipTM=0.89 and pLDDT=63.4 together support a model where the C-terminus docks tightly to KISS1R while the N-terminal 44 residues remain disordered externally, potentially occluding beta-arrestin recruitment.
[2]
noteCard notes KP10/KP13/KP14 are 'minimally active receptor-binding regions', implying KP54 adds significant flanking structure beyond the pharmacophore whose functional role is uncharacterized.
details expand to inspect
full evidence table2 metrics
metricvaluetool
ipTM 0.8898584842681885 boltz-2
ranking score 0.6852999329566956 boltz-2
3-letter notation
Gly-Thr-Ser-Leu-Ser-Pro-Pro-Pro-Glu-Ser-Ser-Gly-Ser-Arg-Gln-Gln-Pro-Gly-Leu-Ser-Ala-Pro-His-Ser-Arg-Gln-Ile-Pro-Ala-Pro-Gln-Gly-Ala-Val-Leu-Val-Gln-Arg-Glu-Lys-Asp-Leu-Pro-Asn-Tyr-Asn-Trp-Asn-Ser-Phe-Gly-Leu-Arg-Phe
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). Kisspeptin-54: natural hormone that triggers puberty and fertility signaling (pep-10561, v1). PeptideModel. https://peptidemodel.com/card/pep-10561
@peptide{pep10561,
  sequence = {GTSLSPPPESSGSRQQPGLSAPHSRQIPAPQGAVLVQREKDLPNYNWNSFGLRF},
  target   = {kiss1r},
  author   = {peptidemodel},
  year     = {2026},
  status   = {synthesized}
}
related peptides 5 by signal overlap
clinical trials 20 on ct.gov · checked 2026-05-09
ct.gov trials 20
with results 5
PubMed RCT 6
by phase
5phase 14phase 21phase 3
by status
6completed3recruiting1terminated
references 69 papers
[1]
Metastin Suppresses the Motility and Growth of CHO Cells Transfected with Its Receptor
Hori, A. et al. Biochemical and Biophysical Research Communications 2001
supporting
[2] supporting
[4] supporting
[5]
Kisspeptin-54 Stimulates the Hypothalamic-Pituitary Gonadal Axis in Human Males
Dhillo, W. et al. The Journal of Clinical Endocrinology & Metabolism 2005
supporting
[10] supporting
[12]
Metastin/Kisspeptin and control of estrous cycle in rats
Maeda, K. et al. Reviews in Endocrine and Metabolic Disorders 2007
supporting
[14] supporting
[16]
Prognostic value of metastin expression in human pancreatic cancer
Nagai, K. et al. Journal of Experimental & Clinical Cancer Research 2009
supporting
[19]
Central administration of metastin increases food intake through opioid neurons in chicks
Khan, M. et al. Comparative Biochemistry and Physiology Part A: Molecular & Integrative Physiology 2009
supporting
[20]
Increased plasma metastin levels in adolescent women with polycystic ovary syndrome
Chen, X. et al. European Journal of Obstetrics & Gynecology and Reproductive Biology 2010
supporting
[24]
Plasma Kisspeptin-54 levels in gastric cancer patients
Ergen, A. et al. International Journal of Surgery 2012
supporting
[26] supporting
[27] supporting
[29] supporting
[30]
Metastin levels in relation with hormonal and metabolic profile in patients with polycystic ovary syndrome
Yilmaz, S. et al. European Journal of Obstetrics & Gynecology and Reproductive Biology 2014
supporting
[32] supporting
[60]
Kisspeptin Excitation of GnRH Neurons
Rønnekleiv, O. et al. Advances in Experimental Medicine and Biology 2013
supporting
[65]
Kisspeptin and Glucose Homeostasis
Izzi-Engbeaya, C. et al. Seminars in Reproductive Medicine 2019
supporting
[67]
The Effects of Kisspeptin-10 on Reproductive Hormone Release Show Sexual Dimorphism in Humans
Jayasena, C. et al. The Journal of Clinical Endocrinology & Metabolism 2011
supporting
discussion no comments
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