# Chonluten

> Chonluten is a synthetic tripeptide, L-glutamyl-L-aspartyl-glycine (Glu-Asp-Gly), with the formula C11H17N3O8 and a molecular weight of 319.27 g/mol. It belongs to the group of short peptide bioregulators and is described in the literature as derived from bronchial epithelial cells. Peer-reviewed data on it are limited to in-vitro work. It is not an FDA-approved drug.

Canonical: https://peptideproperties.com/compounds/chonluten/

## Identity

- **Class:** Short Peptide Bioregulators
- **Also known as:** Glu-Asp-Gly, T-34
- **Molecular formula:** C11H17N3O8
- **Molecular weight:** 319.27 g/mol
- **Monoisotopic mass:** 319.1016 Da
- **CAS number:** 75007-24-8
- **PubChem CID:** 194641
- **InChIKey:** DSPQRJXOIXHOHK-WDSKDSINSA-N
- **Sequence:** EDG
- **Sequence notes:** No modifications; free N-terminal amine and free C-terminal carboxylic acid.

## Key facts

- Class: short peptide bioregulator; synthetic tripeptide
- Sequence: H-Glu-Asp-Gly-OH (EDG), three residues
- Formula C11H17N3O8; molecular weight 319.27 g/mol (PubChem CID 194641)
- CAS 75007-24-8; PubChem synonym: T-34 tripeptide
- Not the same as epitalon (Ala-Glu-Asp-Gly), which has an extra N-terminal alanine
- Evidence base: one in-vitro study in human monocytic THP-1 cells in this source set
- Regulatory status: not approved by the FDA

## What Is Chonluten?

Chonluten is the tripeptide Glu-Asp-Gly, a synthetic short peptide in the group of molecules often called Khavinson peptides or peptide bioregulators. A 2022 study described it as a tripeptide derived from bronchial epithelial cells and noted that peptides in this family were initially isolated from animal tissues and considered organ specific.[1]Peer-reviewed data on Chonluten are limited. A PubMed search returned only one study that clearly examines this compound; most other results for its sequence concerned epitalon (Ala-Glu-Asp-Gly), a different tetrapeptide. This page therefore covers identity facts and the single available study, without extrapolating from related peptides.

## Chemical Structure and Molecular Identity

Chonluten is a linear tripeptide of L-glutamic acid, L-aspartic acid and glycine with free amino and carboxyl termini. PubChem (CID 194641) lists the molecular formula C11H17N3O8, a molecular weight of 319.27 g/mol, the InChIKey DSPQRJXOIXHOHK-WDSKDSINSA-N and CAS number 75007-24-8. PubChem titles the record glutamyl-aspartyl-glycine and lists T-34 tripeptide as a synonym.The molecule is very polar. Three of its residues contribute carboxylic acid groups (two side chains plus the C-terminus), and PubChem gives a computed XLogP of -5.3. Its formula matches the unmodified sequence Glu-Asp-Gly.
### Not to be confused with epitalon
Chonluten's three residues (Glu-Asp-Gly) also appear at positions 2 to 4 of epitalon (Ala-Glu-Asp-Gly). The two are separate compounds with different formulas and molecular weights, and findings reported for epitalon do not apply to Chonluten.

## What the Published Literature Covers

The published record on Chonluten consists of a single in-vitro study, in which it was tested alongside four related peptides in human immune cells. The 2022 study by Avolio, Martinotti, Khavinson and colleagues examined epitalon, vilon, Thymogen, the thymic peptide complex thymalin and Chonluten in the human monocytic leukemia cell line THP-1, which can be differentiated into macrophages in culture.[1]
- Kinase signaling: all five peptides modulated proliferative patterns and increased tyrosine phosphorylation of mitogen-activated cytoplasmic kinases.[1]
- TNF response in monocytes: Chonluten inhibited tumor necrosis factor (TNF) production by monocytes exposed to bacterial lipopolysaccharide (LPS), which the authors linked to a documented mechanism of TNF tolerance.[1]
- Cytokines in macrophages: all peptides inhibited LPS-stimulated expression of TNF and interleukin-6 in terminally differentiated THP-1 cells.[1]
- Cell adhesion: peptide-treated THP-1 cells showed reduced adhesion to LPS-activated human umbilical vein endothelial cells.[1]These are cell-culture results from one research group. No animal studies or human trials of Chonluten were found in the PubMed results reviewed for this page, and no receptor, pharmacokinetic or toxicology data were identified.Because Chonluten differs from epitalon by a single alanine, researchers typically confirm its identity with mass spectrometry and HPLC data on a certificate of analysis.

## Regulatory and Research Status

Chonluten is not approved by the US Food and Drug Administration and is handled as a research compound in the United States. Its peer-reviewed literature is very small, so claims about organ-specific effects in living systems are not supported by independent published data in this source set.Because Chonluten is easily confused with epitalon in searches and on labels, researchers typically confirm that material matches the tripeptide formula C11H17N3O8 and molecular weight 319.27 g/mol rather than the tetrapeptide.

## FAQ

**What is the sequence of Chonluten?**
Chonluten is the tripeptide Glu-Asp-Gly (one-letter code EDG): L-glutamic acid, L-aspartic acid and glycine, with a free N-terminal amine and a free C-terminal carboxylic acid. PubChem (CID 194641) lists its formula as C11H17N3O8 and its molecular weight as 319.27 g/mol, consistent with that unmodified sequence.

**Is Chonluten the same as epitalon?**
No. Chonluten is the tripeptide Glu-Asp-Gly, while epitalon is the tetrapeptide Ala-Glu-Asp-Gly, which carries an extra alanine at the N-terminus. They have different formulas and molecular weights. Many search results for Glu-Asp-Gly sequences actually concern epitalon, and those findings should not be attributed to Chonluten.

**Is Chonluten FDA approved?**
No. Chonluten is not approved by the US Food and Drug Administration for any use and is handled as a research compound in the United States. Its peer-reviewed literature is limited to a single in-vitro study in human monocytic cells, with no published animal studies or human trials identified.

**What does the research on Chonluten show?**
The only study identified tested Chonluten in human THP-1 monocytic cells. It inhibited TNF production by monocytes exposed to bacterial lipopolysaccharide, and, along with four related peptides, reduced LPS-induced TNF and interleukin-6 expression in macrophage-like cells. These are in-vitro findings from one research group and have not been independently replicated.

## References

1. Avolio F, Martinotti S, Khavinson VK, et al. Peptides Regulating Proliferative Activity and Inflammatory Pathways in the Monocyte/Macrophage THP-1 Cell Line. International journal of molecular sciences 2022. PMID: 35408963