Section 01
What it's used for
Osteoarthritis: mostly lab research
Cartalax is a lab-made peptide studied mainly by one Russian institute. In aging cartilage cells, it reduced damage markers. A 2023 review claims animal and patient benefits, but no such study exists, and no human trials are registered.
▸Clinical wording
Cartalax is the trade name of the synthetic tripeptide AED (Ala-Glu-Asp) developed at the St. Petersburg Institute of Bioregulation and Gerontology, and the osteoarthritis literature behind it is preclinical and comes almost entirely from that single Russian group. In an aging chondrocyte culture model, AED normalised the senescence-associated secretory phenotype — the pro-apoptotic proteins p16, p21 and p53 and the pro-inflammatory cytokines TNF-alpha and IL-1alpha are elevated and sirtuin-1 is reduced in aged chondrocytes, and AED shifted these markers back. A 2023 Russian-language review from the same institute states that AED "shown high efficacy in animal models of OA and oral administration in patients with OA of older age groups", but no such animal study or patient trial is indexed in PubMed, so that statement cannot be checked against a primary report. When an international review tabulated Cartalax as a "chondroprotector", the supporting citation was a Russian patent (RU2299741C1), not a published study — there are no registered clinical trials of Cartalax in osteoarthritis.
Cartilage: cell-culture findings only
In human stem cells aged in a dish, this peptide switched on cartilage-building genes at a low dose. Researchers said this only justifies testing in animal models next; no study has checked if it rebuilds cartilage in a living joint.
▸Clinical wording
The most direct cartilage finding is a cell-culture experiment, not a repair study in a living joint. In human mesenchymal stem cells undergoing replicative aging, AED at 200 ng/ml activated both gene expression and protein synthesis of the four chondrogenic markers measured — SOX9, aggrecan, type II collagen and COMP — while the cartilage polypeptide complex required a tenfold higher concentration (2000 ng/ml) for the same effect. The authors themselves present this as grounds for "further investigation of their effectiveness in osteoarthritis models", which means the animal cartilage-repair experiments had not been done at the time of publication. No study has measured whether AED restores cartilage thickness, matrix content or joint function in an animal or a human.
Aging joints: no human data yet
All results come from lab-grown cells, not aging people or animals with joint disease. One rat bone-loss study found a related peptide preserved bone density, though a tissue extract worked better. No human data exist on pain or mobility.
▸Clinical wording
Every published result supporting an anti-aging effect on joint tissue is from cells aged in culture rather than from aging people or animals with joint disease. Alongside the chondrocyte and mesenchymal stem cell work above, one rat study of experimental post-ovariectomy osteoporosis reported an osteoprotective effect on bone mineral density from the peptide substance labelled T-31 — identified as AED in later papers from the same group — although in that experiment the cartilage tissue extract preparation was significantly more effective than the synthetic peptide. There are no published human data on pain, mobility, imaging or function in aging joints, and no independent laboratory outside the originating institute has reproduced these findings.
Cell-aging effects, not cartilage
This peptide's best-studied effects are on aging lab-dish cells, not cartilage. In bone-marrow stem cells it raised a growth protein (IGF1) several-fold. In skin cells it boosted proteins and cut cell death — activity, not proven benefit.
▸Clinical wording
The broadest and most reproducible body of AED data is not about cartilage at all but about gene and protein expression in aging cell cultures of several tissue types. In human embryonic bone-marrow mesenchymal stem cells aged in culture, nanomolar AED raised IGF1 expression 3.5- to 5.6-fold and stimulated NF-kB expression in both aging models tested. In human skin fibroblasts undergoing replicative aging, AED activated synthesis of sirtuin-1, sirtuin-6 and collagen I, inhibited synthesis of the matrix-degrading enzyme MMP-9, and suppressed caspase-dependent apoptosis. All of this is in vitro work from the Khavinson group; it establishes that the peptide does something measurable to cells, not that it produces any clinical effect.
Section 02
Mechanism of Action
How thin the evidence base is
- Cartalax is a three-amino-acid peptide, one constituent of a cartilage extract complex.
- Essentially all primary data come from a single research group and are cell-culture based.
- No independent replication exists, and no human trial of the peptide has been published.
- No published experiment has tested the peptide on cartilage cells at all.
▸Clinical wording
Peptide identity and evidence status
Cartalax is the tripeptide AED (Ala-Glu-Asp). PubMed indexes the name against the supplementary concept "alanyl glutamyl aspartic acid", confirming the identity. AED is one constituent of a polypeptide complex isolated from animal cartilage (PCC) at the St. Petersburg Institute of Bioregulation and Gerontology; that complex contains short peptides of 75-846 Da. Essentially all primary data come from a single research group, are cell-culture based, and have not been replicated independently. No published experiment has tested AED on chondrocytes, and no human trial of AED exists.
A claimed action inside the nucleus
- The originating group proposes that very short peptides enter the nucleus and contact DNA directly.
- A review of that literature claims such peptides interact with DNA and its packaging proteins.
- For this peptide the evidence is computer modelling of binding to a repeating DNA sequence.
- Direct binding to DNA inside cells has not been demonstrated.
▸Clinical wording
Proposed DNA and chromatin interaction
Khavinson's group proposes that ultrashort peptides act by entering the nucleus and contacting DNA and histones directly. A systematic review of this literature states that peptides of 2-7 residues penetrate nuclei and nucleoli and interact with the nucleosome, histone proteins and both single- and double-stranded DNA, including sequence recognition in gene promoters. For AED specifically the evidence is computational: molecular models built alongside the renal cell-culture work indicated that AED forms its energetically most favourable complexes with d(ATATATATAT)2 in the DNA minor groove. Direct binding of AED to DNA in cells has not been demonstrated.
Ageing-related genes shift in cell culture
- In human stem cells aged in culture, the peptide altered expression of ageing-related genes.
- In ageing rat kidney cell culture it raised cell division and lowered three ageing markers.
- In ageing human skin cells it increased two longevity proteins and collagen staining.
- Every observation is in cell culture, read by staining or gene measurement.
▸Clinical wording
Senescence-associated gene expression in cultured cells
In human embryo bone-marrow mesenchymal stem cells (FetMSC line) aged by serial passage or by stationary culture, nanomolar AED altered expression of senescence genes: it stimulated IGF1 and NFkB in both aging models and modulated TNKS2 in the passage model. In ageing rat renal cell culture, AED raised proliferation and lowered the senescence markers p16, p21 and p53 while raising SIRT6. In human skin fibroblasts undergoing replicative aging, AED increased sirtuin-1, sirtuin-6 and collagen I immunostaining. All observations are in vitro, by immunostaining or PCR.
Culture markers of repair and cell death
- In ageing skin cell cultures the peptide blunted the age-related rise of a matrix-degrading enzyme.
- Markers of cell division and regeneration rose, as they did with three related peptides.
- The peptide also suppressed a cell-death enzyme that accumulates as these cultures age.
- The same pattern appeared in rat kidney explants, but weaker than the whole extract complex.
▸Clinical wording
Matrix turnover and apoptosis markers in fibroblast culture
Confocal immunofluorescence in ageing skin fibroblast cultures showed that AED, like the related peptides KE, KED and AEDG, suppressed the age-related rise in MMP-9 and raised the proliferation marker Ki-67 and the regeneration/aging marker CD98hc. AED and AEDG additionally suppressed caspase-dependent apoptosis (caspase-3) that accumulates as these cultures age. The same anti-apoptotic, pro-proliferative pattern was seen in organotypic kidney explants from young and old rats, where AED raised Ki-67 and lowered p53 — though less strongly than the whole polypeptide complex.
The cartilage link is by origin only
- The cartilage connection rests on where the peptide came from, not on cartilage measurements.
- A 2023 review by the originating group argues only that its gene effects "can regulate" stem cell metabolism.
- The peptides that same review lists as actually driving cartilage differentiation are other molecules.
- No study links this peptide to the main cartilage proteins or their degrading enzymes.
▸Clinical wording
Cartilage relevance remains indirect
The connection to cartilage rests on provenance rather than on measured cartilage endpoints. A 2023 review by the originating group places AED inside the cartilage polypeptide complex and argues only that AED's effects on NFkB, IGF1 and TNKS2 "can regulate MSC metabolism and their differentiation" and may translate into reparative properties in cartilage. That same review's survey of peptides shown to drive chondrogenic differentiation of MSCs through WNT, ERK-p38 and Smad 1/5/8 and to raise COL2, SOX9 and ACAN lists other molecules — SK2.1, BMP-derived, B2A, CFOGER, CMP — and not AED. No study links AED to aggrecan, type II collagen, MMP-13 or ADAMTS-5.
Effects seen outside cartilage
- In rats with drug-induced kidney failure, the peptide reduced protein and electrolyte loss in urine.
- A related peptide was the stronger kidney protector in that same experiment.
- In human dental stem cells a four-peptide mixture raised nerve markers, credited to the mixture and another peptide.
- These results bound what the peptide has been shown to do, rather than extend it.
▸Clinical wording
Observations outside cartilage
In rats with cisplatin-induced acute renal failure, AED reduced urinary protein excretion and urine electrolyte concentration, while the related peptide EDL was the more potent nephroprotector in the same experiment. In human periodontal ligament stem cells, a mixture of AEDG, KE, AED and KED raised the neuronal markers GAP43 and nestin, but the effect was attributed to the mixture and to KED alone — AED by itself was not reported to reproduce it. These results are given here to bound the peptide's demonstrated activity, not to extend it.
Section 03
Biological Pathways
- Nuclear DNA and chromatin bindingKhavinson's ultrashort-peptide model holds that short peptides enter the nucleus and bind DNA and histones; modeling placed AED's favored complex in the DNA minor groove, unconfirmed by direct binding in cells.
- Senescence gene modulationIn cultured mesenchymal stem cells AED stimulated IGF1 and NFkB, modulating TNKS2 in one aging model; in aging renal and skin fibroblast cultures it lowered p16, p21 and p53 while raising SIRT6 and sirtuin-1.
- Matrix turnover and apoptosisIn aging skin fibroblast cultures AED suppressed the age-related rise in MMP-9 and caspase-3 while raising Ki-67 and CD98hc; rat kidney explants showed the same anti-apoptotic, pro-proliferative pattern.
- Proposed cartilage relevanceA 2023 review from the originating group argues AED's effects on NFkB, IGF1 and TNKS2 can regulate MSC metabolism, possibly aiding repair, though no study measured AED against collagen II or MMP-13 in cartilage.
Section 04
Dosage Information
Ala-Glu-Asp| Route / system | Context | Range studied | Limitation |
|---|---|---|---|
| Intramuscular — patent case series | Knee arthritis, 29 patients aged 52–72, from the patent | 1 µg, 10 µg or 5 mg once a day for 20 days — three groups, from about 0.011 µg/kg to about 60 µg/kg for a 70–90 kg adult | Pain and movement improved in 54.5–62.7% of cases — no control group, no statistics, nothing published outside the patent. Doses 5,000-fold apart worked alike. |
| Oral — Russian supplement capsules | Maker's leaflet for a capsule sold as a food supplement | 1–2 capsules of 0.215 g, 1–2 times a day with food for 10–30 days, repeated after 4–6 months. The label names no peptide amount. | A leaflet, not a finding: Russian supplement registration involves no efficacy review, and how much of a swallowed peptide reaches the blood is unmeasured. |
| Subcutaneous — self-administration | Practice built around the 20 mg research vial | 1–5 mg a day — roughly 11–70 µg/kg for a 70–90 kg adult — in courses of 10–20 days, two or three times a year | A thousand to five thousand times the 1 µg group in the only human record; the only animal dose under the skin was 0.5 µg per rat. Vial size, not evidence. |
| Cell culture | Human cartilage and stem cells; pieces of rat cartilage | 200 ng/ml where stem cells were turned into cartilage cells; 1, 10, 100, 200 and 400 ng/ml on pieces of cartilage | A concentration in a dish that nothing connects to a blood level after an injection. None of it was ever taken into an animal model of arthritis. |
Results
Syringe Fill Level (100u syringe)
Set positive values for: Recommended dose per kg.
Research Use Only. This information is for educational and research purposes only. Not intended for medical advice or self-medication.
Section 05
Protocols
No protocols featuring this peptide yet. Browse All Protocols
Section 06
Stability & Storage
Storing the product
Cartalax is sold as a finished oral form rather than a lyophilisate: the pack is kept in a dry place away from light at 2–25 °C, with a shelf life of 5 years.
After opening
The instruction sets no separate period once the pack is opened. This form needs no reconstitution, so the conditions after opening are the same as before it.
Section 07
Side Effects & Precautions
No toxicology study, dose-ranging work, or registered clinical trial of the AED tripeptide has been found. What is available are a few safety-related remarks inside efficacy research, and one identity mix-up worth flagging.
Trial data and vendor listings differ from AED
- A Phase I trial cited as showing a safe profile tested the bovine cartilage polypeptide complex, an animal-derived extract, not the AED tripeptide itself.
- AED is only one component identified in that extract, not the tested product, and no clinical trial of AED alone has been reported.
- Vendors also often sell a different molecule, the tetrapeptide AEDL, under the Cartalax name; the substance studied in the literature is the tripeptide AED, not AEDL.
One rat finding, not a safety study
The only in vivo statement about AED itself is inside an efficacy study in old rats: kidney findings were read by the authors as showing no nephrotoxicity. Safety was not the endpoint. No dose is given, and no other organs were examined.
Cartilage evidence is limited to cell cultures
The evidence behind AED's cartilage effects comes from a human stem-cell culture study and a rat chondrocyte culture study. No in vivo osteoarthritis model exists, and no repeat-dose animal study has examined cartilage endpoints, so tolerability of prolonged exposure has never been observed there.
Not registered as a medicine anywhere
The developers' own review lists AED as a chondroprotector supported by a patent, not a study, and does not claim medicinal-product status for it. No marketing authorization for AED was found in any regulator database searched.
No independent confirmation
Every source describing AED, including the kidney finding, comes from the peptide's originating research group or its direct collaborators. Independent reproduction of any of these findings does not exist.
Section 08
Regulatory Status
In Russia it is sold as a dietary supplement under bioregulator rules, not as a registered pharmaceutical, and outside Russia it circulates only as an unapproved research chemical.
FDA / United States
Not approved; sold as a research chemical
Cartalax has no FDA marketing approval and no drug application on record. US and international vendors sell it exclusively as a «research use only» peptide, with explicit disclaimers that it is not intended for human use.
EMA / European Union
No marketing authorisation exists
There is no EU authorisation for Cartalax as a medicine, a novel food or a food supplement. It has not been assessed by the EMA or by any national EU regulator.
Russia
Sold as a supplement, not a registered drug
Developed at the St. Petersburg Institute of Bioregulation and Gerontology, Cartalax is marketed in Russia as a capsule dietary supplement (БАД) through ordinary retail channels. Unlike an approved medicine such as Cortexin, no state pharmaceutical registration number applies to it.
Clinical evidence
No published human trials support its use
Available research is limited to preclinical work from the developer's own institute; independent replication outside that group is essentially absent, and no registered trial has tested Cartalax for cartilage or joint outcomes in people.
WADA
Not named on the list; S0 applies by definition
Cartalax is not listed by name on the WADA Prohibited List, but as a pharmacological substance with no approval anywhere for human therapeutic use, it meets the definition of category S0 (Non-Approved Substances).
A dietary-supplement listing in one country is not a drug approval, and it does not carry over to other jurisdictions. Regulatory status differs between countries and changes over time — check current official sources before relying on any of this.
Section 09
Research Studies
- [1]Gene expression in human mesenchymal stem cell aging cultures: modulation by short peptidesAshapkin V, Khavinson V, Shilovsky G, Linkova N, Vanuyshin B. · Molecular Biology Reports · 2020
- [2]Peptide Regulation of Chondrogenic Stem Cell DifferentiationLinkova N, Khavinson V, Diatlova A, Myakisheva S, Ryzhak G. · International Journal of Molecular Sciences · 2023
- [3]Peptide Regulation of Gene Expression: A Systematic ReviewKhavinson VK, Popovich IG, Linkova NS, Mironova ES, Ilina AR. · Molecules · 2021
- [4]Comparison of the Effects of KE and AED Peptides on Functional Activity of Human Skin Fibroblasts during Their Replicative AgingFridman NV, Linkova NS, Kozhevnikova EO, Gutop EO, Khavinson VK. · Bulletin of Experimental Biology and Medicine · 2020
- [5]Peptide Regulation of Skin Fibroblast Functions during Their Aging In VitroLin'kova NS, Drobintseva AO, Orlova OA, Kuznetsova EP, Polyakova VO, Kvetnoy IM, Khavinson VKh. · Bulletin of Experimental Biology and Medicine · 2016
- [6]Tripeptides slow down aging process in renal cell culture (in Russian)Khavinson VKh, Tarnovskaia SI, Lin'kova NS, Poliakova VO, Durnova AO, Nichik TE, Kvetnoi IM, D'iakonov MM, Iakutseni PP. · Advances in Gerontology · 2014
- [7]Peptide Regulation of Cells Renewal Processes in Kidney Tissue Cultures from Young and Old AnimalsChalisova NI, Lin'kova NS, Nichik TE, Ryzhak AP, Dudkov AV, Ryzhak GA. · Bulletin of Experimental Biology and Medicine · 2015
- [8]Peptides Restore Functional State of the Kidneys During Cisplatin-Induced Acute Renal FailureZamorskii II, Shchudrova TS, Lin'kova NS, Nichik TE, Khavinson VKh. · Bulletin of Experimental Biology and Medicine · 2015
- [9]Effect of short peptides on neuronal differentiation of stem cellsCaputi S, Trubiani O, Sinjari B, Trofimova S, Diomede F, Linkova N, Diatlova A, Khavinson V. · International Journal of Immunopathology and Pharmacology · 2019
Section 10
Frequently Asked Questions
Almost all of the supporting data are laboratory cell-culture experiments from a single research group in St. Petersburg — aging chondrocytes, mesenchymal stem cells and rat kidney cultures — not studies of cartilage repair in a living joint. A 2023 review from that same institute claims "high efficacy in animal models of OA and oral administration in patients," but no such animal study or patient trial is indexed in PubMed, so that specific claim cannot be checked against a primary report. No registered clinical trial of Cartalax in osteoarthritis exists.
A Russian patent describes 29 patients aged 52-72 with knee arthritis, given daily intramuscular injections at one of three doses (1 microgram, 10 micrograms or 5 mg) for 20 days, with pain and movement improving in 54.5-62.7% of cases. There was no control group and no statistical analysis, it was never published outside the patent document, and doses spanning a 5,000-fold range produced similar results — a pattern that doesn't fit a genuine dose-response.
Self-administration outside any study runs at 1-5 mg a day by injection, in 10-20 day courses — a thousand to five thousand times the 1 microgram dose used in the only human case series, and far above the only reported animal dose (0.5 microgram per rat, subcutaneously). The oral supplement capsules sold in Russia don't even state a peptide amount on the label, and Russian supplement registration doesn't require an efficacy review.
The source material lists side effects as "minimal reported" but does not describe any dedicated human safety study, and the regulatory status field is blank, meaning no formal approval status is recorded anywhere. Cancer risk specifically has never been studied for Cartalax — there is simply no data to answer that question either way.
The two aren't studied the same way. BPC-157 has decades of animal injury-model research behind it, even though it too lacks controlled human trials, while Cartalax's evidence base is almost entirely cell cultures from one institute plus a single uncontrolled 29-patient case series described in a patent. The available material does not include any direct comparative study between the two peptides.
As sold, it's a finished oral product rather than a powder needing reconstitution — the pack is kept in a dry place away from light at 2-25°C, with a stated shelf life of 5 years, and the instructions don't set a shorter period once it's opened.