📚 Wiki Weight Loss & Metabolic Leptin Fragment (116-130)

Leptin Fragment (116-130)

● Preclinical
Leptin Peptide Fragment 116-130
Also known as: leptin 116-130, leptin-derived peptide, OB3 peptide
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Quick Summary

Leptin fragment 116-130 is a 15-amino acid peptide derived from the active region of leptin, a 167-amino acid adipokine produced by white adipose tissue. The fragment retains anorexigenic activity of the parent molecule and penetrates the blood-brain barrier more efficiently than full-length leptin due to its smaller size.

Leptin-Derived Peptide Preclinical
leptin/" class="wiki-internal-link">Leptin fragment 116-130 is a 15-amino acid peptide derived from the active region of leptin, a 167-amino acid adipokine produced by white adipose tissue. The fragment retains anorexigenic activity of the parent molecule and penetrates the blood-brain barrier more efficiently than full-length leptin due to its smaller size. In rodent studies, it reduces food intake, promotes weight loss, and improves metabolic parameters in obese animals, suggesting it might circumvent the leptin resistance common in human obesity.
Storage Stability
Lyophilized
1–2 years (-20°C)
Reconstituted
~30 days (2–8°C)
Room temp
Avoid

Mechanism of Action

LepR Receptor Binding and BBB Penetration

Full-length leptin/" class="wiki-internal-link">leptin activates the long-form leptin receptor (LepRb) in the hypothalamus to suppress appetite and increase energy expenditure. Leptin resistance in obesity is partly caused by impaired leptin transport across the blood-brain barrier (BBB). The 116-130 fragment, due to its small size, may use alternative BBB transport mechanisms, potentially bypassing the saturable transport system that limits full leptin.

Hypothalamic Signaling

Leptin fragment 116-130 activates JAK2-STAT3 signaling downstream of LepRb, suppressing NPY/AgRP neurons (orexigenic) and activating POMC/CART neurons (anorexigenic) in the arcuate nucleus. Its hypothalamic activity per mol is lower than full-length leptin but improved CNS delivery may compensate.


Research Summary

Weight Loss in Obese Rodents

Preclinical

In diet-induced obese (DIO) and ob/ob mice, leptin fragment 116-130 administered subcutaneously reduces food intake and body weight comparably to full-length leptin at equivalent molar doses. Importantly, some studies show activity in leptin-resistant DIO animals where full leptin is ineffective, supporting the BBB penetration hypothesis.

Metabolic Parameters

Preclinical

Chronic administration in rodent models improves fasting glucose, insulin sensitivity, and reduces hepatic steatosis. Adipose tissue lipolysis increases. These effects mirror full leptin's metabolic actions at similar CNS leptin receptor engagement.


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Research Protocols

GoalDoseFrequencyRoute
Appetite suppression (obese rodent)0.1-1 mg/kg SCDailySubcutaneous
Weight loss (DIO mouse)0.5 mg/kg IPDaily x 14 daysIntraperitoneal
BBB penetration assessmentRadiolabeled fragmentSingle doseIV + brain quantification

No human clinical data. All protocols are rodent research. Leptin fragment 116-130 is not available as a clinical compound.


Interactions

complementary
Both suppress appetite via hypothalamic circuits; nesfatin-1 pathway is leptin-independent
complementary
GLP-1 agonists
Convergent appetite suppression and weight loss; different receptor systems
synergistic
Insulin
Leptin and insulin co-signal in the hypothalamus for energy balance; improved insulin sensitivity may be additive

Safety Profile

No human safety data. Full-length leptin has been tested in clinical trials for lipodystrophy (metreleptin is FDA-approved) and obesity, showing generally good tolerability but limited efficacy in common obesity due to leptin resistance. Fragment 116-130 has no human data. Theoretical concerns include immune responses to a self-derived fragment sequence and potential off-target receptor activation.


References

  • [1]Grasso P, et al. Intranasal administration of leptin(116-130) inhibits food intake and produces weight loss in lean, obese, and leptin-resistant mice. Exp Biol Med. 2011;236(5):474-478.
  • [2]Zhang F, et al. Crystal structure of the obese protein leptin-E100. Nature. 1997;387(6629):206-209.
  • [3]Banks WA, et al. Leptin enters the brain by a saturable system independent of insulin. Peptides. 1996;17(2):305-311.
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Verified Scientific Data Last audited:
Data Sources & External References
Source: peer-reviewed literature  ·  Domain: ascendpeptide.org

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