Chonluten Research, Specifications & Scientific Information

Introduction

Chonluten is the smallest peptide in the Khavinson bioregulator series: Glu-Asp-Gly, three residues, 319 daltons.

It is also the hardest of them to find in the literature, for reasons that are entirely bibliographic. It appears under three labels — the trade name, the sequence EDG, and the laboratory code T-34 — and each returns a different fraction of the record. Only one indexed paper uses the trade name in its abstract at all ^[1]. And its sequence sits inside Ala-Glu-Asp-Gly, which is Epitalon, so a text search for the tripeptide returns a large volume of tetrapeptide work that has nothing to do with it.

What survives that filtering is three primary papers, and one of them reports the compound doing nothing where four siblings acted ^[3]. That negative result is on this page rather than left off it, because it is the most informative single fact about this molecule.

The family's shared limitations apply and are stated once here: a single originating research programme and its collaborators, small studies, no clinical report of any design, no whole-animal study of this compound located at all, and no independent replication.

What Is Chonluten?

A synthetic tripeptide with free termini, EDG in single-letter code: L-alpha-glutamyl-L-alpha-aspartyl-glycine. PubChem carries it as compound identifier 194641 under CAS registry number 75007-24-8, and lists T-34 tripeptide among its synonyms — which is the link that makes the coded literature findable.

Its tissue assignment is not settled between the sources that give one. The 2022 monocyte paper describes the tripeptide as derived from bronchial epithelial cells ^[1]. The originating group's own 2022 review table lists it instead under gastroprotection and stress protection ^[4]. A compound described as bronchial in one source and gastric in another, by overlapping authors, is one whose tissue assignment should be treated as a label rather than as a finding.

Chonluten has not been approved by the U.S. Food and Drug Administration for any indication. No marketing application is on record in the United States, and no study of it appears on ClinicalTrials.gov.

Chonluten Specifications

PubChem carries the free tripeptide as compound identifier 194641 with CAS registry number 75007-24-8, formula C11H17N3O8 and an average mass of 319.27 g/mol; the record lists the laboratory code T-34 as a synonym, which is the label most of the primary literature uses. No unique ingredient identifier resolves in the FDA/NCATS Global Substance Registration System. At 319 daltons this is the smallest tripeptide in the Khavinson series and one of the smallest molecules in this library with a literature of its own. A search hazard applies: Glu-Asp-Gly is a substring of Ala-Glu-Asp-Gly, the sequence of Epitalon, so a text search on the tripeptide returns a large number of tetrapeptide papers that are not about this compound, and the three labels — trade name, sequence and code — each return a different fraction of the real record.

Values that a public register does not carry are shown as not publicly characterised rather than estimated. Identifiers are reference values; the certificate of analysis supplied with a laboratory order is the record for a given lot.

How Does Chonluten Work?

Not established. No receptor has been identified, none is proposed, and the specification table shows primary target, receptor family and agonist status as not publicly characterised.

The signalling observations come from the monocyte work described in the tiered section below: increased tyrosine phosphorylation of mitogen-activated cytoplasmic kinases, reduced lipopolysaccharide-stimulated output of tumour necrosis factor and interleukin-6, and reduced adhesion to activated endothelium, which the authors read together as induction of tumour necrosis factor tolerance ^[1]. Kinase phosphorylation is a proximal readout by the standards of this literature, and it is still downstream of whatever the peptide did first.

The gene-expression paper needs a caveat about what it does not say. A 2012 report states that the peptide, under its laboratory code, regulates messenger RNA expression for a range of genes, that the development of gastric ulcer is associated with morphological and molecular changes arising from altered synthesis of antioxidant and anti-inflammatory proteins, and that the peptide normalises the synthesis of those proteins by regulating the corresponding genes ^[2]. The indexed abstract does not state what system the measurements were made in — whether cultured cells, excised tissue or an intact animal. Because the tier cannot be determined from the published record, that study is described here under the mechanism heading and is not assigned an evidence tier anywhere on this page.

No transport, no pharmacokinetics, and no whole-animal study. In every experiment located, the peptide was added to a culture medium or to an excised explant. Nothing is published about what happens to it in an organism.

Chonluten Mechanism of Action

In vitro research

Monocytes and macrophages. Five preparations of the series were tested together in the human monocytic THP-1 line, which differentiates into macrophages on exposure to phorbol ester: this tripeptide, Epitalon, Vilon, Thymogen and the extract Thymalin ^[1].

All five increased tyrosine phosphorylation of mitogen-activated cytoplasmic kinases. All five reduced expression of tumour necrosis factor and of interleukin-6 stimulated by bacterial lipopolysaccharide in terminally differentiated cells. All five reduced adhesion of the treated cells to endothelial monolayers activated with lipopolysaccharide. This tripeptide is the one the abstract singles out, for inhibiting tumour necrosis factor production by lipopolysaccharide-exposed monocytes — a pattern the authors connect to the documented phenomenon of tumour necrosis factor tolerance.

Two cautions. When five structurally unrelated preparations — two dipeptides, a tripeptide, a tetrapeptide and an undefined extract — all produce the same effect in the same assay, the shared result says at least as much about the assay as about any one of them. And the paper is a collaboration involving the originator of the series, so it is not independent replication, whatever its Italian co-authorship suggests at first glance.

The negative result in skin explants. Five synthesised tripeptides were tested in organotypic skin cultures from young and old rats: T-32 (Glu-Asp-Ala), T-33 (Glu-Asp-Arg), T-34 (Glu-Asp-Gly), T-36 (Glu-Asp-Pro) and T-38 (Lys-Glu-Asp). In explants from young rats, all peptides except T-34 produced a stimulating effect on cell proliferation. In explants from old rats, T-38 produced a marked stimulatory effect, with immunocytochemistry attributing the increase to reduced expression of the proapoptotic p53 protein ^[3].

This compound is the exception in that experiment, and the paper's own conclusion — that the capacity of the studied tripeptides to promote proliferation justifies further study — does not single it out. A member of a series that fails where its four closest analogues succeed is evidence that the sequences are doing something different from one another, which is the series' own claim; it is also a result that no summary of this compound elsewhere mentions.

Findings in this section were obtained in cultured cells and in excised tissue. None of them establishes anything about an intact animal, and none about a person.

What Is Chonluten Being Researched For?

• Inflammatory signalling in monocytes and macrophages — tumour necrosis factor and interleukin-6 output, kinase phosphorylation and endothelial adhesion ^[1].
• Expression of antioxidant and anti-inflammatory genes — under the laboratory code, in a system the indexed record does not specify ^[2].
• Comparative tripeptide activity in explant culture — where this compound was the inactive member of five ^[3].

No other research area has an identifiable primary literature for this compound. None of the above is research into, or evidence about, research-grade material supplied for laboratory use.

Current Research Status

Status as of September 22, 2026. This block is rendered from maintained fields, not from prose, so it cannot go stale in one place and stay current in another.

Chonluten vs Related Compounds

Epitalon :: Ala-Glu-Asp-Gly — this exact sequence with an alanine added at the front. The relationship is the source of the search problem described above, and it is also the sharpest structural question this compound raises: a tripeptide and its own N-terminal extension are assigned to different tissues by the series, and no experiment testing the two against each other has been located. Pinealon, Crystagen and Vesugen :: T-33, T-36 and T-38 in the coded literature — three of the four tripeptides that acted in the skin explant experiment where this one did not ^[3]. Bronchogen :: The other lung-assigned peptide of the series, the tetrapeptide Ala-Glu-Asp-Leu, with a substantially larger literature including a rat model and direct DNA-binding measurements. Two compounds from one programme assigned to the same tissue is unusual, and the division of labour between them is not explained anywhere in the published record. Vilon, Thymogen and Thymalin :: The other three preparations in the monocyte experiment, all of which produced the same effects ^[1].

Evidentiary position

Not approved by the U.S. Food and Drug Administration, no registered trial, no clinical report of any design, no whole-animal study located, and three primary papers in total.

No comparison of effect between these compounds is made on this page.

Chemical & Molecular Characteristics

This is the smallest and most acidic molecule in the batch. Three residues, 319 daltons, and glycine — the one standard amino acid with no side chain at all — occupying a third of the sequence. The glutamate side chain, the aspartate side chain and the C-terminal carboxyl give three ionisable acidic groups against a single N-terminal amine. The result is a strongly anionic, extremely water-soluble molecule with no hydrophobic surface whatsoever.

Nothing about it retains on a reversed-phase column. A 319-dalton peptide this polar elutes at or near the void volume on conventional C18, in the region where salts, residual reagents and small synthesis by-products also appear. For this compound more than any other on this list, a bare "purity by HPLC" figure without the method behind it carries almost no information, and ion-pairing, mixed-mode or hydrophilic-interaction separation is what would be needed to say anything.

No aromatic residue, so no absorbance at 280 nm. Quantification relies on peptide-bond absorbance near 214 nm, where solvents and buffers also absorb.

Glycine at the C-terminus removes the last steric constraint. With no side chain there, the backbone around that residue is maximally flexible; there is essentially no conformational preference anywhere in this molecule. Whatever selectivity it has does not come from shape.

Adjacent acidic residues make isomerisation the identity question, and there is nothing else to check it against. Glutamate followed by aspartate is the motif most prone to alpha/beta and alpha/gamma rearrangement under heat and acid. The rearranged species have the same molecular formula and the same mass. In a molecule of only three residues, with no aromatic handle, no hydrophobic retention and no register unique ingredient identifier, the analytical margin for error is unusually narrow — and a mass spectrum reporting 319.27 daltons confirms composition and nothing about connectivity.

One register field is empty. CAS registry number 75007-24-8 and PubChem compound identifier 194641 both resolve; no FDA/NCATS unique ingredient identifier does. That field is shown as unknown above rather than filled from a neighbouring substance.

Frequently Asked Questions

Scientific 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 doi:10.3390/ijms23073607
2. Khavinson VKh, Lin'kova NS, Dudkov AV, et al.. Peptidergic regulation of expression of genes encoding antioxidant and anti-inflammatory proteins Bulletin of experimental biology and medicine; 2012. PMID 22803148 doi:10.1007/s10517-012-1590-2
3. Voicekhovskaya MA, Chalisova NI, Kontsevaya EA, et al.. Effect of bioregulatory tripeptides on the culture of skin cells from young and old rats Bulletin of experimental biology and medicine; 2012. PMID 22803085 doi:10.1007/s10517-012-1527-9
4. Khavinson V, Linkova N, Kozhevnikova E, et al.. Transport of Biologically Active Ultrashort Peptides Using POT and LAT Carriers International journal of molecular sciences; 2022. PMID 35887081 doi:10.3390/ijms23147733

Every identifier above is resolved against PubMed, Crossref or ClinicalTrials.gov at build time, and the title returned by the register is compared with the title stored here. A page does not publish if a reference fails to resolve.

Research-Use Information

For in vitro research use only. This material is a laboratory reagent. It is not a drug, food, dietary supplement, or cosmetic and is not for human or veterinary use, including ingestion, injection, or any other administration. No information on this page describes or implies any effect in humans or animals. Sold only to researchers under our Terms of Sale.