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Compound Evidence InstituteEvidence synthesis · established 2023Graded assessments of compounds, trials, methods and supply
Document set current to 30 July 2026
Compound monograph · §2

Kisspeptin-10 — pharmacology

Molecular targets, mechanism of action, pharmacokinetics and interactions as characterised in humans.

Document identifier
CEI-MN-050/2
Series
Compound monograph
Version
2.2
Published
11 Jun 2025
Last reviewed
11 Jun 2025
Next review
11 Jun 2027
Identifier
10.71829/cei.mono.50
Certainty
Low
Cycle
2025 Q2

§2Pharmacology

§2.1Molecular targets

Table 2. Molecular targets recorded for Kisspeptin-10, with the character of the interaction and the potency where the Institute holds it.

TargetInteractionNote
KISS1 receptor (KISS1R, GPR54)AgonistExpressed on hypothalamic GnRH neurons; the master regulator of GnRH pulsatility

§2.2Mechanism of action

Kisspeptin acts on KISS1 receptors on hypothalamic gonadotropin-releasing hormone neurons to stimulate GnRH secretion, and thereby luteinising hormone and follicle-stimulating hormone release. Because it acts upstream of GnRH it preserves the pulsatile architecture of the axis, which distinguishes it from continuous GnRH agonist administration. Its principal clinical research applications are as a diagnostic probe of hypothalamic function and as an alternative trigger for oocyte maturation in assisted reproduction.[1,2]

§2.3Pharmacokinetics

Terminal half-life
≈4 min
Time to maximum concentration
immediate on infusion
Volume of distribution
not published
Plasma protein binding
not extensively bound
Clearance
high
Bioavailability
not established for subcutaneous administration

Rapid proteolysis. The very short half-life confines use to infusion or bolus in a controlled setting.

Reconstructed plasma concentration–time profilePlasma concentration plotted against time after dosing, reconstructed from published pharmacokinetic parameters.0.00.20.40.60.801122Time after first dose (hours)Relative concentrationt max ≈ 0 ht½ ≈ 1 h
Modelled profileSimulated observationsDose administration
Figure 2. Illustrative. Plasma concentration–time profile reconstructed by the Institute from the published half-life and time-to-maximum-concentration parameters using a one-compartment model with first-order absorption. The curve is not digitised from a published figure and its vertical scale is relative. It is published to convey the shape of the profile and the approach to steady state, not to supply a concentration at any time point.

§2.4Interactions

  • Not characterised

References cited on this page

References are numbered in order of first citation in this document. Each superscript in the text links to its entry below.

  1. D’Hondt M, Bracke N, Taevernier L, Gevaert B, Verbeke F, Wynendaele E, De Spiegeleer B. Related impurities in peptide medicines. Journal of Pharmaceutical and Biomedical Analysis 2014;101:2–30. doi:10.1016/j.jpba.2014.06.012 · PMID 25044089
  2. Manning MC, Chou DK, Murphy BM, Payne RW, Katayama DS. Stability of protein pharmaceuticals: an update. Pharmaceutical Research 2010;27(4):544–575. doi:10.1007/s11095-009-0045-6 · PMID 20143256

Identifiers are reproduced only where the Institute holds them. Where a digital object identifier or PubMed identifier is not shown, the Institute has recorded the journal and year and has not constructed an identifier.

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