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Professor Peptides
Research compound

Chonluten

Also known as Chonluten · Chonluten tripeptide

Bronchial-derived tripeptide that suppressed TNF and IL-6 in monocyte cultures

Last reviewed · Educational reference — not medical advice.

Half-life
Not characterised in published pharmacokinetic studies
Route
Subcutaneous or intramuscular in the source literature
Status
Research compound — short peptide bioregulator
Mechanism
Reported to induce TNF tolerance in monocytes: suppression of TNF and IL-6 expression after lipopolysaccharide stimulation, together with reduced monocyte adhesion to activated endothelium. Proposed to act through the same nuclear/epigenetic route as the rest of this peptide family, though this was not directly demonstrated for Chonluten.
01

Overview

Chonluten is described in the peer-reviewed literature as a tripeptide derived from bronchial epithelial cells, and it is one of five Khavinson peptides characterised head-to-head in a 2022 study on the human monocytic THP-1 line.

That study produced the most specific finding attached to this compound. Chonluten inhibited tumour necrosis factor (TNF) production in monocytes exposed to bacterial lipopolysaccharide. Reduced TNF release from LPS-stimulated monocytes is a recognised mechanism known as TNF tolerance, which attenuates inflammatory response. All five peptides tested inhibited LPS-stimulated TNF and IL-6 expression in terminally differentiated THP-1 cells and reduced their adhesion to LPS-activated endothelium, but the TNF result was highlighted specifically for Chonluten, whose bronchial epithelial origin the authors noted.

Sequence caveat: vendor listings commonly state Chonluten as Glu-Asp-Gly (EDG). No indexed source located in this research confirms that. The 2022 study establishes only that it is a tripeptide of bronchial epithelial origin. PubChem's Glu-Asp-Gly entry does not list Chonluten among its synonyms. The sequence is therefore recorded here as unconfirmed rather than asserted.

Research areasMonocyte and macrophage inflammatory signallingTNF toleranceBronchial epithelial peptide biologyPeptide regulation of gene expression
02

What the evidence shows

Separated by study type
HumanClinical trials and human studies
No controlled clinical trials. The cell line used (THP-1) is human-derived, but no human subject has been studied.
AnimalRodent and other animal models
No indexed animal outcome studies.
In vitroCell and tissue studies
Inhibited TNF production in LPS-exposed monocytes, consistent with a TNF-tolerance mechanism; suppressed LPS-stimulated TNF and IL-6 expression in terminally differentiated THP-1 cells; reduced THP-1 adhesion to LPS-activated HUVEC endothelium; increased tyrosine phosphorylation of mitogen-activated cytoplasmic kinases.
03

Key studies & findings

2 studies
  1. 1

    Chonluten, a tripeptide derived from bronchial epithelial cells, inhibited TNF production in monocytes exposed to bacterial LPS in vitro — a documented TNF-tolerance mechanism that attenuates inflammatory action.

    In vitro2022International Journal of Molecular Sciences, 2022 (opens in new tab)

  2. 2

    All five Khavinson peptides tested (epitalon, Vilon, thymogen, thymalin, Chonluten) suppressed LPS-stimulated TNF and IL-6 expression in terminally differentiated THP-1 cells and reduced adhesion to activated endothelium.

    In vitro2022International Journal of Molecular Sciences, 2022 (opens in new tab)

04

Benefits & effects

3 documented

  • Inhibition of TNF production in LPS-stimulated monocytes

    Verified

  • Suppression of IL-6 expression in differentiated THP-1 cells

    Verified

  • Reduced monocyte adhesion to activated endothelium

    Verified
05

Side effects & safety

1 reported

Safety noteResearch compound for laboratory use only. No regulatory safety review, no established human safety database, and no controlled toxicology data in the public literature.

Recorded in the cited literature No controlled human safety data exist for this compound.

  • Amino acid sequence unconfirmed — material identity cannot be verified against a public reference

    unknown
06

Limitations & open questions

Nearly all published work on this compound originates from a single research programme (the St Petersburg Institute of Bioregulation and Gerontology, Khavinson group) and its collaborators. Independent replication outside that network is sparse to non-existent, sample sizes are small, and much of the source literature is published in Russian-language journals with limited peer-review transparency. Effects reported in cell culture and in aged-donor lymphocytes have not been shown to produce clinical outcomes in controlled human trials. Specific to Chonluten: its amino acid sequence is not stated in any indexed source located in this research. Vendors commonly list it as Glu-Asp-Gly, but PubChem's Glu-Asp-Gly record does not name Chonluten as a synonym, so that assignment is unverified. Buyers cannot confirm what they are receiving against a public reference.

07

Pharmacology

Chonluten is described as a tripeptide of bronchial epithelial origin. No PubChem record could be matched to the trade name in this session, no CAS number was confirmed, and no pharmacokinetic study exists. Molecular formula and weight are therefore not stated here.

08

Frequently asked questions

What is Chonluten's amino acid sequence?

Not confirmed. Vendors list it as Glu-Asp-Gly (EDG), but no indexed source found in this research states the sequence, and PubChem's Glu-Asp-Gly entry does not list Chonluten as a synonym. The peer-reviewed literature establishes only that it is a tripeptide of bronchial epithelial origin.

What is TNF tolerance?

A state in which monocytes exposed to an inflammatory trigger such as bacterial LPS release less TNF than they otherwise would, dampening the inflammatory response. Chonluten was reported to induce this in cultured monocytes.

Does this mean Chonluten is anti-inflammatory in people?

It has not been tested in people. The finding is a cytokine measurement in a cultured monocyte line, which is several steps removed from a clinical anti-inflammatory effect.

09

Citations

2 sources
  1. 1
    Peptides Regulating Proliferative Activity and Inflammatory Pathways in the Monocyte/Macrophage THP-1 Cell Line (opens in new tab)Avolio F, Martinotti S, Khavinson VKh, Esposito JE, Giambuzzi G, et al. (2022) · doi:10.3390/ijms23073607
  2. 2
    Peptide Regulation of Gene Expression: A Systematic Review (opens in new tab)Khavinson VKh, Popovich IG, Linkova NS, Mironova ES, Ilina AR (2021) · doi:10.3390/molecules26227053