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LEAP-2

● Preclinical; under investigation as obesity therapeutic target
Liver-Expressed Antimicrobial Peptide 2 (LEAP-2)
Also known as: Liver-Expressed Antimicrobial Peptide 2, GHSR1a endogenous antagonist
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Quick Summary

LEAP-2 (Liver-Expressed Antimicrobial Peptide 2) was originally identified as a hepatic antimicrobial peptide but gained major research attention in 2018 when it was discovered to be a potent endogenous antagonist and inverse agonist of the ghrelin receptor (GHSR). Where ghrelin activates GHSR to drive hunger, fat storage, and growth hormone release, LEAP-2 blocks these effects.

Hepatokine / Metabolic Peptide Active Research
LEAP-2 (Liver-Expressed Antimicrobial Peptide 2) was originally identified as a hepatic antimicrobial peptide but gained major research attention in 2018 when it was discovered to be a potent endogenous antagonist and inverse agonist of the ghrelin/" class="wiki-internal-link">ghrelin receptor (GHSR). Where ghrelin activates GHSR to drive hunger, fat storage, and growth hormone release, LEAP-2 blocks these effects. LEAP-2 is produced by the liver and small intestine in response to feeding, high fat diet, and elevated glucose, the opposite pattern to ghrelin, which rises during fasting. LEAP-2/ghrelin ratios fluctuate with feeding state and obesity, with obese individuals showing a relative LEAP-2 excess that may contribute to impaired ghrelin signaling. LEAP-2 is emerging as a counterbalancing signal in the ghrelin system relevant to obesity, appetite, and GH regulation.
Storage Stability
Lyophilized
1–2 years (-20°C)
Reconstituted
~30 days (2–8°C)
Room temp
Avoid

Mechanism of Action

Ghrelin Receptor Antagonism

LEAP-2 binds GHSR1a (the active ghrelin/" class="wiki-internal-link">ghrelin receptor) with high affinity and blocks ghrelin binding, acting as a competitive antagonist. Beyond simple blockade, LEAP-2 acts as an inverse agonist, suppressing the constitutive (ligand-independent) activity of GHSR1a. GHSR1a has one of the highest constitutive activities of any known GPCR (~50% basal signaling without ligand), which drives baseline hunger signaling. LEAP-2 suppression of this constitutive activity reduces hunger tone independent of circulating ghrelin.

Postprandial Regulation

LEAP-2 is secreted from hepatocytes and enterocytes in response to glucose, insulin, and lipids, signals of adequate nutrition. Its postprandial rise opposes ghrelin's fasting-induced rise, creating a complementary see-saw. As a meal-responsive GHSR antagonist, LEAP-2 contributes to meal termination and postprandial satiety signaling. This function was overlooked before the receptor connection was made; LEAP-2 is now considered a genuine counter-regulatory hormone to ghrelin.

Growth Hormone Regulation

By blocking GHSR1a in the hypothalamus and pituitary, LEAP-2 reduces ghrelin-stimulated growth hormone release. Elevated LEAP-2 in obesity may partly explain the blunted GH pulse amplitude and reduced IGF-1 seen in obese individuals. LEAP-2 also suppresses ghrelin-driven GH secretion during sleep, potentially contributing to the obesity-associated disruption of nocturnal GH peaks.


Research Summary

Appetite and Obesity

Preclinical

LEAP-2 administration reduces food intake and body weight in diet-induced obese mice, even when ghrelin is absent (via inverse agonism at constitutive GHSR activity). LEAP-2 knockout mice show increased GHSR-dependent feeding, hyperphagia, and greater obesity susceptibility. In humans, plasma LEAP-2 rises with BMI, though whether this represents pathological compensatory elevation or causative signaling is being studied.

LEAP-2/Ghrelin Ratio

Clinical Biomarker

The molar LEAP-2/ghrelin ratio is a more informative biomarker of metabolic state than either hormone alone. During fasting, low LEAP-2 and high ghrelin create a high ratio of GHSR activation. In obesity, elevated LEAP-2 and suppressed ghrelin may impair the normal hunger signaling that regulates meal patterns. This ratio may predict response to ghrelin-system therapies and bariatric surgery outcomes.

Alcohol Use and Neurological

Emerging

GHSR plays roles in reward, motivation, and alcohol seeking behavior. LEAP-2 reduces ghrelin-driven alcohol preference in rodent models, suggesting it may modulate addictive behaviors mediated by the ghrelin/GHSR system. Central LEAP-2 effects on dopamine reward circuits via GHSR are an emerging research area with implications for addiction and mood disorders.


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Research Protocols

GoalDoseFrequencyRoute
Appetite suppression (rodent)10-50 mg/kg SCOnce daily for 1-2 weeksSC
GH suppression study1-10 mg/kg IVAcute; measure GH at 15, 30, 60 minIV bolus
GHSR binding assay1-1000 nMConcentration-response curveIn vitro receptor binding

Human dosing not yet established. LEAP-2 is in early preclinical-to-clinical translation with most data from rodent models.


Interactions

Direct antagonist
Ghrelin
LEAP-2 blocks ghrelin at GHSR1a and suppresses constitutive GHSR activity, primary counter-regulatory relationship
Inverse agonist
GHSR1a
LEAP-2 suppresses both ghrelin-stimulated and constitutive GHSR1a signaling
Complementary
Both rise postprandially and suppress appetite via distinct mechanisms (GLP-1R vs GHSR antagonism)
Indirect
IGF-1
LEAP-2 reduces GH release, lowering IGF-1 over time, relevant in GH deficiency contexts

Safety Profile

LEAP-2 has no established human safety profile. Rodent studies show reduced food intake and body weight as primary effects without gross toxicity. Suppression of constitutive GHSR activity raises theoretical concerns about overly suppressing GH pulsatility, which could impair muscle maintenance and metabolic rate over the long term. The rapid receptor action of LEAP-2 suggests short-term use for appetite control would be different from chronic GH suppression. No hepatotoxicity, cardiovascular, or immunological adverse effects noted in current animal studies.


References

  • [1]Ge X, et al. LEAP2 is an endogenous antagonist of the ghrelin receptor. Cell Metab. 2018;27:461-469.
  • [2]M'Kadmi C, et al. LEAP2 inhibits ghrelin-stimulated GH secretion and food intake. Mol Cell Endocrinol. 2019.
  • [3]Muller TD, et al. Ghrelin. Mol Metab. 2015.
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Data Sources & External References
Source: peer-reviewed literature  ·  Domain: ascendpeptide.org

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