Cartalax (AED)

Three residues, and a fourth that belongs to another peptide

The molecule is Ala-Glu-Asp: alanine, glutamic acid, aspartic acid, nothing appended. PubChem holds it as CID 87815447 with the molecular formula C12H19N3O8 and a molecular weight of 333.29 g/mol, listing Cartalax and T-31 peptide among its synonyms. MeSH carries the same compound as supplementary concept C572340, alanyl-glutamyl-aspartic acid, with cartalax as an entry term, which is why a PubMed search on the trade name returns the AED literature rather than nothing. That search returned six records on 18 August 2026. The registry trail ends at chemical databases. A query of the FDA Global Substance Registration System returns no substance record and no UNII, and UniChem returns no ChEMBL entry.

The CAS number needs its provenance stated. 85806-95-7 appears in PubChem's depositor-supplied synonyms, and tracing it through the eleven substance records attached to the compound places it in exactly one: a deposit from a commercial chemical supplier. No governmental or regulatory depositor attests it, PubChem prints no separate CAS heading for the record, and CAS Common Chemistry could not be queried without an API key. It is carried on this page with that qualification rather than as a verified identifier. The comparison is instructive: the closely related tripeptide pinealon carries its CAS inside an EPA DSSTox depositor entry, which is a different grade of attestation.

Product listings and aggregator pages print a different molecule. The sequence they overwhelmingly assign to Cartalax is Ala-Glu-Asp-Leu, a tetrapeptide of roughly 446 Da. AEDL is bronchogen in the originating laboratory's own publications. A 2012 study in Bulletin of Experimental Biology and Medicine names bronchogen (Ala-Glu-Asp-Leu) as the peptide that stimulated CXCL12 and Hoxa3 in human bronchial epithelial cells, and a 2017 tobacco callus paper in Biochemistry (Moscow) spells the sequence out the same way. Khavinson's 2022 review in the International Journal of Molecular Sciences lists both compounds in one table, on separate rows, with separate docking scores.

A second sequence error sits inside the databases themselves. The MeSH record's entry terms include H-Asp-Glu-Asp-OH, which is aspartic acid rather than alanine at the first position, and that string has propagated into the synonym list for PubChem CID 87815447. Anyone checking the sequence against either source can arrive at the wrong N-terminal residue without ever leaving a primary database. Three sequences therefore circulate under one name — AED in the literature, AEDL on vendor pages, and DED inside two reference databases — and a search engine summary generated during work on this page supplied a fourth, AEDG, which is epitalon.

The chondroprotector label traces to a patent

Khavinson's 2022 transport review contains the clearest statement of what this compound is supposed to do. Its second table ranks twenty-seven ultrashort peptides by docking score against LAT1, the human L-type neutral amino acid transporter, and the Cartalax row reads: Cartalax (AED), ICM-Score minus 26.65, biological activity Chondroprotector [167] and Regulation of skin fibroblast functions [168]. The second reference is a paper — Fridman 2020, the skin fibroblast study. The reference attached to the cartilage word is not. It is RU2299741C1, a Russian patent titled Peptide Normalizing Metabolism in Bone and Cartilaginous Tissues, filed 30 May 2006 by Khavinson, Grigoriev, Malinin and Ryzhak as inventors, with a limited company as applicant, and granted 27 May 2007. The review's own reference list misdates that grant to 27 May 2008.

The 2023 chondrogenic review from the same group also cites a patent, Eurasian Patent EA 010574 of 30 October 2008, but for a narrower point — that AED is one of the short peptides making up the cartilage polypeptide complex. Only the 2022 review attaches a patent to the chondroprotector designation itself. A patent carries no protocol, no arm sizes, no randomisation and no analysis, and it is the only citation offered for the organ assignment. The docking score beside it is a number produced in software: Cartalax sits seventh of twenty-seven, between Ovagen (EDL) at minus 28.27 and Thymogen (EW) at minus 24.72, with Bronchogen (AEDL) far below at minus 17.26. A companion 2023 paper in Biomolecules compared all 8,400 di- and tripeptides against LAT1, LAT2 and PEPT1 and reported that the twenty-six named peptides score higher than sequences with no established activity. No experimental transport measurement for AED was located.

The 2023 review reaches cartilage by analogy, and says so. It surveys nine peptides for chondrogenic differentiation of mesenchymal stem cells — B2A, the CK2 series, SPPEPS, KLD-12, an N-cadherin mimetic, RGD, GFOGER, LPP and collagen mimetic peptides — none of which come from this programme. AED enters through gene expression measured in stem cells and skin fibroblasts, and the bridging sentence states that chondrocytes have similarities in structure and function with fibroblasts and that the fibroblast data may also demonstrate reparative properties in cartilage tissue. Read as written, that is a hypothesis the authors flag as one.

What has actually been measured in cartilage cells

Two publications put this peptide on cartilage-lineage cells, and both appeared in 2023 in the same Russian journal. Myakisheva and colleagues applied AED and a cartilage polypeptide complex to human mesenchymal stem cells during replicative ageing and reported that AED at 200 nanograms per millilitre activated gene expression and protein synthesis of SOX9, aggrecan, type II collagen and COMP, the four standard chondrogenic markers. The polypeptide complex reached the same effect at 2,000 nanograms per millilitre. A companion paper characterised the senescence-associated secretory phenotype of chondrocytes as raised p16, p21, p53, TNF-alpha and IL-1-alpha with lowered Sirt1, and reported that both substances normalised those molecules.

Neither abstract states a sample size. Neither gives a donor count, a passage range, a replicate number, an effect size, a control compound or any description of blinding. Both are Russian-language reports in Advances in Gerontology, neither is open access, and full texts could not be retrieved from PubMed Central, Europe PMC or the publisher for this page. What is quoted above is the entirety of what the indexed record makes available on the only experiments that have paired this molecule with cartilage biology.

PubMed searches on 18 August 2026 for the string Ala-Glu-Asp combined with cartilage, and combined with chondrocyte, each returned zero records; the two 2023 papers use the abbreviation AED in their English abstracts and do not surface on the spelled-out sequence. No animal model of osteoarthritis has been published with this tripeptide in any language indexed by PubMed or Europe PMC. Cartilage thickness, proteoglycan content, histological grading and joint function have not been measured in any animal after administering it. The absent searches carry as much of this page as the two positive papers do.

The kidney, where most of the in vivo work sits

The rodent work on AED is renal. Zamorskii and colleagues gave a kidney polypeptide complex and the peptides AED, EDL and AEDG to rats with cisplatin-induced acute renal failure and reported that AED decreased protein excretion and electrolyte concentration in the urine. The same abstract records that the complex and the peptides EDL and AEDG normalised diuresis, creatinine concentration, glomerular filtration rate and sodium handling, and names EDL as the potent nephroprotective agent. AED is the one entry in that list credited with the narrowest set of changes. Group sizes, doses and route appear nowhere in the abstract.

A 2018 study from the same collaboration measured old rats without an injury model. Administration of the kidney complex and the peptides AED and EDL raised diuresis by 1.2 to 1.4 times; the complex and AED lowered urine protein concentration and protein excretion by 1.5 to 2.8 times; distal sodium transport rose 1.2 to 1.3 times, and sodium excretion rose 1.3 times under AED and 1.6 under EDL. Antioxidant enzyme activity in kidney tissue rose while peroxidation fell, which the authors read alongside morphology as absence of nephrotoxicity. The abstract states no dose, no route and no group size.

Culture work in the same tissue is more granular and no better documented. In organotypic kidney explants from young and old rats, the polypeptide complex raised Ki-67 and reduced p53; T-31, the internal code for AED, was reported only to stimulate proliferation and reduce apoptosis, and the abstract states plainly that the effect was smaller than that of the complex. In renal cell culture, AED and EDL reduced p16, p21 and p53 and raised SIRT-6, and the authors built molecular models placing both peptides in the minor groove of d(ATATATATAT)2. That paper reports a measurement and a docking calculation, and treats the second as the mechanism for the first.

Skin, stem cells, and one flat result

Fibroblast experiments are the strongest part of this record and are frequently borrowed to speak for cartilage. Confocal immunofluorescence work published in 2016 reported that AED, alongside KE, KED and AEDG, inhibited MMP-9 synthesis and raised Ki-67 and CD98hc in ageing skin fibroblast cultures, and that AED and AEDG suppressed caspase-dependent apoptosis. A 2020 comparison in human skin fibroblasts during replicative ageing reported that AED activated synthesis of sirtuin-1, sirtuin-6 and collagen I. Type I collagen is the skin protein. The collagen of hyaline cartilage is type II, and the two are not interchangeable.

The stem cell results point in more than one direction. In human embryo bone marrow mesenchymal cells, AED, KED and KE raised IGF1 expression 3.5 to 5.6 fold across two ageing models and all three stimulated NF-kappa-B expression; the 2023 review's own reading of that second result runs in both directions within a single paragraph, proposing that the effect on NF-kappa-B accelerates stem cell ageing and that it may reduce inflammation in osteoarthritis. A 2019 study in the International Journal of Immunopathology and Pharmacology applied AED, KED, KE and AEDG to human periodontal ligament stem cells and reported that GAP43 and nestin rose under the compound of all four peptides and under KED alone; AED on its own is credited with neither.

One published test of this peptide found nothing. Applying T-31 alongside two other coded peptides to old passage-eight thymocyte cultures, Lin'kova and colleagues reported in 2011 that only AB-9 exhibited a geroprotective effect, stimulating proliferation and differentiation and inhibiting apoptosis. T-31 is named in the methods and absent from the results. Negative findings are scarce in this programme, and the one that exists is worth recording alongside the rest.

The bone experiment, and what belongs to the extract

Only one in vivo study has approached the skeletal claim. Povorozniuk and colleagues reported in 2007 that a preparation based on cartilaginous tissue extract and the substance T-31 were each osteoprotective in ovariectomised rats, preventing loss of bone mineral density and raising density that ovariectomy had reduced. The abstract also states that the extract was significantly more effective than the peptide. It gives no group size, no dose, no route and no duration, it is a Russian-language report in Advances in Gerontology, and it is not open access. That is the whole of the in vivo skeletal record, and the tripeptide came second in it.

The only human data in this area concern the extract. Sigumir, the polypeptide complex of cartilage and bone tissue, carries a 2012 report on 62 patients with temporomandibular joint disease that PubMed types as a Clinical Trial, in which the complex was one component of a package including prosthetics and pharmacotherapy. The 2023 chondrogenic review states that the complex is in the second phase of clinical trials for osteoarthritis in Russia. No registration number accompanies that sentence, and searches of ClinicalTrials.gov for the compound, the complex, the investigator and the institute each returned zero studies.

Cartalax is not an approved medicine in any jurisdiction. It holds no UNII and no ChEMBL entry, and it was not among the seven substances the FDA Pharmacy Compounding Advisory Committee considered for the section 503A bulks list on 23 and 24 July 2026; that agenda covered BPC-157, KPV, TB-500, MOTS-c, emideltide, semax and epitalon. Publication types were checked on every paper cited here and none carries a retraction, an expression of concern or an erratum, which distinguishes this record from several others in the category.

What is not known

No registered trial of this compound exists anywhere. Searches of ClinicalTrials.gov on 18 August 2026 returned zero studies for cartalax that were not fuzzy matches on unrelated enteral nutrition and antiepileptic drug records, zero for sigumir, zero for cartilage polypeptide complex, and zero for both the investigator and the originating institute; a control query on Ala-Glu-Asp returned 116 unrelated amino acid trials, confirming the endpoint was responding. Nothing is established about absorption, distribution, metabolism or clearance in any species, so no administered amount can be related to any tissue concentration, and the culture concentrations in the record cannot be converted into anything else. Whether the tripeptide survives oral administration intact has not been measured, and the transport argument offered in its place is a docking score. Immunogenicity, reproductive and developmental toxicity, chronic exposure, genotoxicity and carcinogenicity have not been assessed. Group sizes are absent from every primary abstract on this page without exception, several of which are Russian-language reports in one journal describing neither randomisation, blinding, nor a placebo arm, and none of which is open access. Where the tripeptide has been compared directly against the polypeptide complex it came from, in ovariectomised rats and in kidney explants, the complex was the more effective of the two. The whole record originates with one institute in St Petersburg and its collaborators; the Italian and Ukrainian groups that appear as coauthors did so alongside that institute, and no independent replication of any finding was located. Cartalax is not an approved medicine in any jurisdiction, holds no UNII and no ChEMBL entry, and material sold outside a registered trial has been subject to no identity, purity or sterility control — a point sharpened here by the fact that the sequence most commonly printed on such material is not the sequence in the literature.

Questions