Cartalax is the trade name used for a synthetic tripeptide, a chain of just three amino acids: alanine, glutamic acid and aspartic acid. In the scientific literature it appears as AED (Ala-Glu-Asp) or by its laboratory code T-31. It comes from Vladimir Khavinson’s group at the St. Petersburg Institute of Bioregulation and Gerontology in Russia, which describes it as a “bioregulator” of cartilage and bone. Online it is marketed for joint health and “anti-aging.”
The single most important fact: no controlled human trial of AED has been published in the indexed literature, and nearly every study comes from one research group. The evidence consists of cell-culture experiments, a few rat studies, and a Russian review that mentions use in older patients with osteoarthritis without giving trial data. Cartalax is not an FDA-approved drug.
This page summarizes what the published laboratory and animal studies report. It is for education only and is not medical advice.
| Property | Detail |
|---|---|
| Class | Synthetic tripeptide (Ala-Glu-Asp); one of the Khavinson “peptide bioregulators” |
| Other names | AED, T-31, Kartalax, L-alanyl-L-glutamyl-L-aspartic acid |
| Formula and weight | C₁₂H₁₉N₃O₈, 333.29 g/mol (PubChem) |
| CAS number | 85806-95-7 |
| Origin | Identified as a component of a polypeptide complex extracted from animal cartilage |
| Human data | No published controlled trials; a 2023 Russian review mentions oral use in older adults with osteoarthritis without reporting results |
| Half-life | Unknown. We found no published pharmacokinetic study in humans or animals |
| Proposed mechanism | Changes in gene and protein expression in cultured cells; the group proposes direct binding to DNA, based on computer modeling |
| US status | Not an FDA-approved drug; no approved product found in FDA’s drug database |
| WADA | Not named on the 2026 list; class S0 covers substances with no government approval for human therapeutic use |
What it is
AED is the tripeptide L-alanyl-L-glutamyl-L-aspartic acid. PubChem lists “Cartalax” and “T-31 peptide” as synonyms of the same compound (PubChem). Its three amino acids are the same as the first three of epitalon, the four-amino-acid pineal peptide from the same group, but the two are separate compounds with separate research.
According to a 2023 review by the Khavinson group, AED is one of the short peptides found in a polypeptide complex extracted from animal cartilage at their institute. The review states that this cartilage complex, not AED itself, was in phase 2 clinical trials for osteoarthritis in Russia (Linkova et al., Int J Mol Sci 2023). A related cartilage-and-bone extract called Sigumir is discussed alongside AED in the same group’s reviews (Myakisheva et al., Adv Gerontol 2023).
Cartalax belongs to a family of short peptides the group has promoted as tissue-specific bioregulators. Others in the library include thymalin, thymagen, vilon, pinealon and epitalon.
How it works in the body
Nobody has shown how AED acts in people. The group’s proposed mechanism is that short peptides cross cell and nuclear membranes and bind DNA directly, switching genes on or off. This idea rests on computer docking models, which predicted that AED binds a specific short DNA sequence (Khavinson et al., Bull Exp Biol Med 2016). The authors themselves wrote that the molecular mechanism “remains unclear.” Docking models predict binding; they do not show that it happens inside living cells.
Pharmacokinetics
We found no published study measuring AED’s absorption, distribution, half-life or excretion, in people or in animals. Whether any intact AED reaches cartilage after oral or injected use has not been reported. Half-life figures quoted online are not based on published measurements.
Regulatory status
- Not an approved drug in the US. A search of FDA’s drug approvals database (Drugs@FDA, via openFDA) returned no product containing cartalax. We found no FDA or EMA approval.
- Not on FDA’s compounding safety-risk list. FDA’s page on bulk substances that may pose significant safety risks names several research peptides, including epitalon, but did not name cartalax when we checked (FDA, 2026). This does not mean it has been reviewed or found safe.
- Sport. AED is not named on the 2026 WADA Prohibited List. Class S0 bans, at all times, any pharmacological substance “with no current approval by any governmental regulatory health authority for human therapeutic use” (WADA 2026 Prohibited List). We found no WADA ruling specific to AED.
What the research shows
Every study below involves Khavinson or his institute’s staff as authors. We found no independent replication. Several are short Russian-language papers for which only an abstract is available.
Human evidence
We found no published randomized or controlled trial of AED in humans. A 2023 Russian-language review states that the cartilage extract Sigumir and the AED tripeptide “have shown high efficacy” in animal models of osteoarthritis and with oral use in older patients with osteoarthritis (Myakisheva et al., Adv Gerontol 2023). The abstract gives no number of patients, dose, duration, control group or outcome measure, and we could not locate the underlying patient study. This claim cannot be evaluated.
Cartilage and stem cells in culture
| Study | Cells | Reported finding |
|---|---|---|
| Myakisheva et al., Adv Gerontol 2023 | Human mesenchymal stem cells (cells that can become cartilage, bone or fat) during replicative aging | AED at 200 ng/mL raised gene expression and protein synthesis of cartilage markers (SOX9, aggrecan, type II collagen, COMP); the cartilage extract needed 2,000 ng/mL for the same effect |
| Myakisheva et al., Adv Gerontol 2023 | Aging chondrocytes (cartilage cells) | AED and the cartilage extract “normalize” aging and inflammation markers (p16, p21, p53, TNF-α, IL-1α, Sirt1); no figures in the abstract |
| Ashapkin et al., Mol Biol Rep 2020 | Human fetal bone-marrow stem cells in two aging models | AED, KED and KE at nanomolar concentrations raised IGF1 gene expression 3.5–5.6-fold and raised NF-κB gene expression |
Skin and kidney cells in culture
| Study | Cells | Reported finding |
|---|---|---|
| Fridman et al., Bull Exp Biol Med 2020 | Human skin fibroblasts during replicative aging | AED increased sirtuin-1, sirtuin-6 and type I collagen |
| Lin’kova et al., Bull Exp Biol Med 2016 | Aging skin fibroblasts | AED and other peptides lowered MMP-9 and raised proliferation markers; AED reduced caspase-dependent apoptosis (programmed cell death) |
| Khavinson et al., Adv Gerontol 2014 | Young and aged kidney cells | AED raised proliferation, lowered aging markers p16, p21 and p53, and raised SIRT-6 |
| Khavinson et al., Bull Exp Biol Med 2014; Chalisova et al., Bull Exp Biol Med 2015 | Kidney cell and tissue cultures from rats | AED stimulated cell renewal and reduced apoptosis, but less than the calf-kidney extract it was compared with |
Not every result was positive. In aging thymus cell cultures, AED (T-31) was tested with two other peptides, and only one of the others showed the full set of effects the authors looked for (Lin’kova et al., Bull Exp Biol Med 2011). In a study of nerve-cell differentiation of human dental stem cells, the marker GAP43 rose with a mix of four peptides and with KED alone; the abstract does not report this effect for AED alone (Caputi et al., Int J Immunopathol Pharmacol 2019).
All of these results come from cells in a dish. Most studies measured marker proteins by staining and microscopy, the abstracts rarely give numbers, and none tested whether the changes translate into healthier tissue.
Animal studies
| Model | Main reported result |
|---|---|
| Ovariectomized rats, a model of postmenopausal bone loss (Povorozniuk et al., Adv Gerontol 2007) | T-31 and a cartilage extract both prevented loss of bone mineral density; the extract was significantly more effective than T-31 |
| Old rats (Zamorskii et al., Adv Gerontol 2018) | AED, a related peptide (EDL) and a kidney extract raised urine output 1.2–1.4-fold; AED and the extract lowered urine protein 1.5–2.8-fold; tissue findings were read as showing no kidney toxicity |
| Rats with cisplatin-induced acute kidney failure (Zamorskii et al., Bull Exp Biol Med 2015) | AED lowered urine protein and electrolytes; another peptide, EDL, had the strongest protective effect |
We found no published animal study of AED in an osteoarthritis model with reported numbers, despite the review’s statement that it was effective in such models. Doses, routes and group sizes are not given in these abstracts.
Side effects and risks
No human safety data
No published study has systematically assessed AED’s safety in people. There are no reported toxicology studies (acute, repeat-dose, reproductive or genotoxicity), no dose-response data, and no drug interaction data. Its effects in pregnancy, breastfeeding, children and people with kidney, liver or autoimmune disease are unknown. The absence of reported side effects in the group’s papers is not evidence of safety, because none was designed to detect them.
Product quality
Products sold online as Cartalax are not regulated drugs in the US. Their identity, purity, dose per capsule or vial, and (for injectable forms) sterility are not independently verified. Injected peptides with impurities or aggregates can trigger immune reactions, a concern FDA has raised for similar research peptides such as epitalon (FDA, 2026).
Gene-expression claims cut both ways
The group’s own data show AED raising IGF1 and NF-κB gene expression in stem cells (Ashapkin et al., Mol Biol Rep 2020). NF-κB is a central switch for inflammation, and IGF-1 signaling promotes cell growth. Whether these changes are beneficial, harmful or irrelevant in a living person has not been studied.
Key takeaways
- A three-amino-acid peptide. Cartalax is the trade name for AED (Ala-Glu-Asp), also called T-31, developed by Khavinson’s group in St. Petersburg as a cartilage “bioregulator.”
- Not an approved drug. We found no FDA or EMA approval, and WADA’s S0 class bans substances without any government approval for human therapy.
- No published human trials. The only human claim is one sentence in a 2023 Russian review, with no patient numbers, doses or outcomes.
- Evidence is from one research group. Every cell and animal study we found involved the same institute, mostly in short papers with abstract-only data and no independent replication.
- Laboratory results only. AED changed cartilage, skin and kidney cell markers in culture and protected bone and kidney measures in a few rat studies, often less effectively than the tissue extracts it was compared with.
- Pharmacokinetics and safety are unknown. No half-life, absorption or toxicology data have been published.
Sources
- National Center for Biotechnology Information. PubChem compound summary for CID 87815447, Cartalax (Ala-Glu-Asp). PubChem.
- Linkova N, Khavinson V, Diatlova A, et al. Peptide Regulation of Chondrogenic Stem Cell Differentiation. Int J Mol Sci. 2023;24(9):8415. PubMed.
- Myakisheva SN, Linkova NS, Kozhevnikova EO, Ryzhak GA. Chondrocytes secretory phenotype associated with aging: role in the pathogenesis of osteoarthritis and prospects for peptide bioregulation. In Russian. Adv Gerontol. 2023;36(3):313–323. PubMed.
- Myakisheva SN, Linkova NS, Diatlova AS, et al. The influence of peptides on the chondrogenic differentiation of human mesenchymal stem cells during replicative aging. In Russian. Adv Gerontol. 2023;36(3):383–390. PubMed.
- Myakisheva SN, Linkova NS, Kozhevnikova EO, et al. Peptides prevent the forming of secretory phenotype of chondrocytes associated with the aging. In Russian. Adv Gerontol. 2023;36(2):234–238. PubMed.
- Ashapkin V, Khavinson V, Shilovsky G, et al. Gene expression in human mesenchymal stem cell aging cultures: modulation by short peptides. Mol Biol Rep. 2020;47(6):4323–4329. PubMed.
- Fridman NV, Linkova NS, Kozhevnikova EO, et al. Comparison of the Effects of KE and AED Peptides on Functional Activity of Human Skin Fibroblasts during Their Replicative Aging. Bull Exp Biol Med. 2020;170(1):154–157. PubMed.
- Lin’kova NS, Drobintseva AO, Orlova OA, et al. Peptide Regulation of Skin Fibroblast Functions during Their Aging In Vitro. Bull Exp Biol Med. 2016;161(1):175–178. PubMed.
- Khavinson VK, Lin’kova NS, Tarnovskaya SI. Short Peptides Regulate Gene Expression. Bull Exp Biol Med. 2016;162(2):288–292. PubMed.
- Khavinson VKh, Tarnovskaia SI, Lin’kova NS, et al. Tripeptides slow down aging process in renal cell culture. In Russian. Adv Gerontol. 2014;27(4):651–656. PubMed.
- Khavinson VKh, Lin’kova NS, Polyakova VO, et al. Peptides regulate expression of signaling molecules in kidney cell cultures during in vitro aging. Bull Exp Biol Med. 2014;157(2):261–264. PubMed.
- Chalisova NI, Lin’kova NS, Nichik TE, et al. Peptide Regulation of Cells Renewal Processes in Kidney Tissue Cultures from Young and Old Animals. Bull Exp Biol Med. 2015;159(1):124–127. PubMed.
- Lin’kova NS, Polyakova VO, Trofimov AV, et al. Peptidergic regulation of thymocyte differentiation, proliferation, and apoptosis during aging of the thymus. Bull Exp Biol Med. 2011;151(2):239–242. PubMed.
- Caputi S, Trubiani O, Sinjari B, et al. Effect of short peptides on neuronal differentiation of stem cells. Int J Immunopathol Pharmacol. 2019;33:2058738419828613. PubMed.
- Povorozniuk VV, Khavinson VKh, Makogonchuk AV, et al. Effect of peptide regulators on the structural and functional status of bone tissue in ageing rats. In Russian. Adv Gerontol. 2007;20(2):134–137. PubMed.
- Zamorskii II, Shchudrova TS, Zeleniuk VG, et al. The influence of peptides on the morphofunctional state of old rats kidneys. In Russian. Adv Gerontol. 2018;31(4):498–504. PubMed.
- Zamorskii II, Shchudrova TS, Lin’kova NS, et al. Peptides Restore Functional State of the Kidneys During Cisplatin-Induced Acute Renal Failure. Bull Exp Biol Med. 2015;159(6):736–739. PubMed.
- Food and Drug Administration. Certain bulk drug substances for use in compounding that may present significant safety risks. Accessed October 2026. FDA.
- World Anti-Doping Agency. The 2026 Prohibited List. In effect January 1, 2026. WADA.