Cartalax (AED Peptide) – Research Compound Profile

Cartalax (AED Peptide) – Research Compound Profile

Category: Musculoskeletal Research | Molecular Type: Synthetic Tripeptide Bioregulator (Ala-Glu-Asp) | Research Status: Preclinical & In Vitro (Limited Observational Human Data)

This page compiles published research data for qualified researchers. Cartalax is sold exclusively as a research compound and is not approved for human use.

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Molecular Overview

Cartalax is a synthetic tripeptide bioregulator with the amino acid sequence Ala-Glu-Asp (commonly abbreviated “AED”), developed by Prof. Vladimir Khavinson at the St. Petersburg Institute of Bioregulation and Gerontology as part of a broader family of ultrashort organ-specific peptides [1]. Its molecular formula is C₁₂H₁₉N₃O₈ with a molecular weight of 333.29 g/mol [8]. The AED amino acid sequence corresponds to a motif found within the alpha-1 chain of type XI collagen (COL11A1), a structural protein essential for organizing the collagen fibril network in articular cartilage [2]. This structural homology is hypothesized to underpin Cartalax’s tissue specificity — research indicates preferential activity in connective tissue cells including chondrocytes, fibroblasts, and renal epithelial cells [2][3][10].

Cartalax belongs to the Khavinson class of bioregulatory peptides — ultrashort synthetic molecules (2–7 amino acids) that have been studied for over 35 years as part of a peptide bioregulation research program originating in Russia [1][11]. A polypeptide complex from cartilage (PCC), which contains the AED peptide among its active components, has been reported to have reached Phase II clinical investigation in Russia, providing context for laboratory interest in the AED sequence [2].

Structurally, Cartalax is among the smallest molecules in this class. At three residues it has no appreciable secondary structure, and its behaviour is dominated by its two acidic side chains: glutamate and aspartate give it strongly anionic character at neutral pH and an acidic isoelectric point, accounting for its high aqueous solubility. It contains no cysteine, so there is no disulfide chemistry to preserve, and no methionine or tryptophan, the two residues most prone to oxidation.

Mechanism of Action

Unlike conventional pharmaceuticals that bind cell-surface receptors, Khavinson peptides such as Cartalax are proposed to operate at the nuclear level. The small molecular size of the AED peptide allows it to penetrate cell membranes and reach chromatin targets, where it has been observed to bind specific nucleotide sequences and influence transcriptional activity [5][7][8]. A 2021 systematic review by Khavinson et al. described how short peptides (2–7 amino acids) penetrate nuclei and interact with nucleosomes to regulate transcription, establishing the theoretical framework for Cartalax’s mechanism [5].

At the molecular level, Cartalax has been studied across multiple cell types:

Chondrocyte Regulation: In a 2024 Bulletin of Experimental Biology and Medicine study, Linkova, Khavinson et al. examined the AED peptide’s effect on primary rat chondrocytes. At an effective concentration of 200 ng/mL, the peptide increased chondrocyte numbers in cultures from both young (3-month) and old (24-month) animals by 1.4–1.6-fold. The peptide boosted the cartilage area index by 18–38%, stimulated proliferating cell nuclear antigen (PCNA) expression, and reduced p53 protein synthesis in cartilage tissue cultures [4].

Fibroblast Modulation: In aging fibroblast replicative models, Lin’kova et al. (2016) reported that Cartalax increased Ki-67 (a proliferation marker) and CD98hc (a regeneration-associated glycoprotein) while simultaneously suppressing caspase-3 (the executioner protease of apoptosis) and MMP-9 (a matrix metalloproteinase that degrades extracellular matrix components) [3].

Mesenchymal Stem Cell Gene Expression: In a 2020 Molecular Biology Reports study, Ashapkin et al. demonstrated that in human mesenchymal stem cell (MSC) aging cultures, the AED peptide modulated expression of IGF1 (insulin-like growth factor 1), FOXO1, TERT (telomerase reverse transcriptase), TNKS2 (tankyrase 2, involved in telomere maintenance and Wnt signaling), and NFκB, with expression changes ranging from 1.6-fold to 5.6-fold compared to untreated controls [9].

Renal Epithelial Cell Senescence: Khavinson et al. (2014) reported that in renal epithelial cell cultures, the AED peptide decreased expression of the senescence markers p16, p21, and p53 while upregulating SIRT6, a sirtuin deacetylase associated with genomic stability and cellular longevity [10].

Epigenetic Regulation: Ashapkin et al. (2015) demonstrated how short peptides, including AED, regulate cellular differentiation through epigenetic modulation of gene expression during aging in human cells [12].

Interpretive limits of the nuclear-binding model: Direct sequence-specific binding of a tripeptide to double-stranded DNA is a weak interaction by the standards of transcription-factor biochemistry, and published support rests largely on molecular modelling and in vitro binding work rather than structural determination in cells [5][7]. Alternative explanations — indirect signalling, effects on peptide-transport systems, or contribution of the constituent amino acids after hydrolysis — have not been formally excluded. The gene-expression data are internally consistent across several cell types, which is the strongest feature of the evidence base; the causal chain from peptide to chromatin remains the weakest, and independent replication outside the originating research group is limited.

Published Research Parameters

The following table indexes the experimental models, durations, and reported observations of the peer-reviewed publications cited on this page. It is a bibliographic index, not a protocol, and contains no recommendation for any use.

Note: Essentially all published Cartalax (AED) data derives from in vitro cell culture and animal models. No peer-reviewed randomized controlled trials in humans have been published, and the compound has no established clinical evidence base. Every observation on this page is a laboratory finding in a specific model system.

Stability & Storage Characteristics

Published guidelines and peptide chemistry literature provide the following stability data relevant to Cartalax:

• Lyophilized form: Lyophilized peptides of this class demonstrate long-term stability when stored at −20 °C (−4 °F). Short-term storage at 2–8 °C (35.6–46.4 °F) is considered acceptable for periods of weeks [6].
• Reconstituted solution: Peptide solutions are generally recommended for storage at 2–8 °C (35.6–46.4 °F) and are typically considered stable for up to 4 weeks under these conditions [6].
• Freeze-thaw sensitivity: Repeated freeze-thaw cycles are documented to degrade tripeptide integrity and should be avoided [6].
• Light sensitivity: UV exposure degrades peptide bonds; storage protected from direct light is standard practice for peptides of this class [6].
• Molecular characteristics: With a molecular weight of 333.29 g/mol and the simple Ala-Glu-Asp sequence, Cartalax is expected to follow general stability patterns for short peptides in the absence of specific published degradation kinetics [8]. Its two acidic residues make it highly water-soluble, so co-solvents are not required for reconstitution.
• Principal degradation routes: The expected chemical liabilities are hydrolysis of the two amide bonds and cyclisation chemistry at the aspartate residue — Asp-containing sequences are susceptible to succinimide formation and iso-aspartate rearrangement in aqueous storage, yielding a species of identical mass but altered structure. Buffer pH is therefore a more important variable than for a neutral peptide.

Analytical Characterization

Confirming the identity and purity of a tripeptide requires a different panel from that used for longer peptides. Reverse-phase HPLC remains the primary purity method, but a small, doubly anionic molecule is weakly retained on C18 chemistry, so ion-pairing agents or hydrophilic-interaction chromatography are generally needed. Electrospray mass spectrometry confirms the molecular ion against the expected 333.29 g/mol, though because the iso-aspartate rearrangement product is mass-identical to the parent, mass alone cannot establish structural integrity. Amino-acid analysis after complete hydrolysis confirms the 1:1:1 residue ratio. Net peptide content should be distinguished from gross vial mass, since counter-ion and residual water are a significant fraction of weighed material at this molecular weight.

Key Published Research Findings

All findings below are derived from the cited peer-reviewed publications. Each observation is attributed to the specific study in which it was reported.

• Chondrocyte proliferation (age-independent): In a 2024 Bulletin of Experimental Biology and Medicine study using primary rat chondrocyte cultures, Linkova, Khavinson et al. observed that the AED peptide at 200 ng/mL increased chondrocyte numbers by 1.4–1.6-fold in cultures derived from both young (3-month) and aged (24-month) animals, demonstrating activity independent of donor age [4].

• Cartilage tissue area expansion: In the same 2024 study, the cartilage area index increased by 18–38% in tissue culture models treated with the AED peptide, alongside stimulation of PCNA expression and suppression of p53 protein synthesis [4].

• Anti-senescence gene modulation in MSCs: In a 2020 Molecular Biology Reports study, Ashapkin et al. reported that the AED peptide produced 1.6–5.6-fold changes in expression of IGF1, FOXO1, TERT, TNKS2, and NFκB in human mesenchymal stem cell aging cultures — genes implicated in cellular aging, telomere maintenance, and metabolic regulation [9].

• Extracellular matrix preservation: In a 2016 Bulletin of Experimental Biology and Medicine study, Lin’kova et al. demonstrated that the AED peptide inhibited MMP-9 synthesis in aging fibroblast cultures. MMP-9 is a matrix metalloproteinase that degrades collagen and proteoglycans in the cartilage matrix during aging [3].

• SIRT6 upregulation and senescence marker suppression: In a 2014 Advances in Gerontology study, Khavinson et al. observed that the AED tripeptide decreased p16, p21, and p53 expression while increasing SIRT6 in renal epithelial cell cultures — a molecular profile associated with genomic stability and cellular longevity [10].

• Fibroblast proliferative and anti-apoptotic effects: Lin’kova et al. (2016) reported Ki-67 upregulation and caspase-3 suppression in aging fibroblast cultures treated with the AED peptide, indicating both pro-proliferative and anti-apoptotic properties in this model system [3].

• Lifespan extension in animal models: In a 2009 Biogerontology review, Anisimov and Khavinson reported that long-term treatment with Khavinson peptide bioregulators increased mean lifespan by 20–40% in animal models, providing broader context for the geroprotective potential of this peptide class [11].

Safety Profile in Published Literature

• Class-level safety data: Khavinson bioregulatory peptides as a class have been studied over 35+ years of preclinical and clinical observation in Russia without reports of significant systemic adverse events [1][11].
• Limited adverse event reporting: In observational settings for Khavinson bioregulator peptides, the most commonly reported effect has been mild, transient local reactions at administration sites [1].
• Absence of formal pharmacokinetic data: No published pharmacokinetic characterization of Cartalax exists — half-life, bioavailability, and distribution are unreported. Cell-culture findings therefore cannot be extrapolated to whole-organism exposure.
• No controlled clinical trials: No placebo-controlled, double-blinded clinical trials have been conducted for Cartalax. Most safety data derives from the broader Khavinson bioregulator research program and the related PCC (polypeptide complex from cartilage) clinical trials [2].
• Toxicology: No published reports of significant systemic toxicity were identified in the reviewed literature for the AED peptide specifically or for the broader Khavinson short peptide class [1][11].

Regulatory Status

• FDA approval: Cartalax (AED peptide) is not FDA-approved for any therapeutic indication. It is not classified as a drug, dietary supplement, or approved biologic in the United States.
• Clinical trial status: The polypeptide complex from cartilage (PCC), which contains the AED peptide among its active components, has been reported to have reached Phase II clinical investigation in Russia [2]. That work concerns a different, multi-component preparation and does not extend to Cartalax, for which no ClinicalTrials.gov registrations were identified and which no regulatory authority has evaluated.
• Research compound classification: Cartalax is sold exclusively as a research compound for in vitro and laboratory use. It is not intended for human consumption, therapeutic use, or self-administration.
• Russian regulatory context: Khavinson bioregulatory peptides have a longer regulatory history in Russia, where certain formulations have been available as dietary supplements or registered through the Russian regulatory framework. This status does not confer approval in other jurisdictions [1].

Research Use Only

All information on this page is provided for informational and citation purposes and summarizes findings from published scientific literature. Cartalax (Ala-Glu-Asp-Gly, AED) supplied by IronPeak Peptides LLC is intended for laboratory research purposes only. It is not a drug, food, or cosmetic, is not intended for human or veterinary consumption, and is not intended to diagnose, treat, cure, or prevent any disease. Nothing on this page constitutes medical advice or a recommendation for use in humans. Handling should be performed only by qualified researchers in an appropriate laboratory setting.

References

1. Neuroendocrinology Letters (2002) — Khavinson VK. Peptides and Ageing. Overview of bioregulatory peptide development and geroprotective mechanisms across 35+ years of research. View Source

2. International Journal of Molecular Sciences (2023) — Linkova N, Khavinson V, Diatlova A, Myakisheva S, Ryzhak G. Peptide Regulation of Chondrogenic Stem Cell Differentiation. Comprehensive review of AED peptide’s role in chondrocyte regulation and MSC differentiation pathways. View Source

3. Bulletin of Experimental Biology and Medicine (2016) — Lin’kova NS, Drobintseva AO, Orlova OA, et al. Peptide Regulation of Skin Fibroblast Functions during Their Aging In Vitro. Demonstrated AED peptide effects on Ki-67, CD98hc, caspase-3, and MMP-9 in aging fibroblast models. View Source

4. Bulletin of Experimental Biology and Medicine (2024) — Linkova NS, Khavinson VK, et al. Peptides of Cartilage Tissue: Regulation of Chondrocyte Proliferation, Geroprotection, and Prospects for Use in Osteoarthrosis. AED peptide at 200 ng/mL increased chondrocyte numbers 1.4–1.6× in young and old rat cultures. View Source

5. Molecules (2021) — Khavinson VK, Popovich IG, Linkova NS, Mironova ES, Ilina AR. Peptide Regulation of Gene Expression: A Systematic Review. Short peptides (2–7 amino acids) penetrate nuclei and interact with nucleosomes to regulate transcription. View Source

6. Bachem (Peptide Handling Guide) — Handling and Storage Guidelines for Peptides. Lyophilized peptides stable at −20 °C; reconstituted solutions at 2–8 °C; avoid freeze–thaw cycles. View Source

7. Advances in Gerontology (2016) — Khavinson VK, Lin’kova NS, Tarnovskaya SI. Short Peptides Regulate Gene Expression. Signal molecules regulating organism functions at molecular, genetic, and cellular levels. View Source

8. PubChem — Compound Summary for Cartalax (AED peptide; CID 87815447). Molecular formula C₁₂H₁₉N₃O₈, molecular weight 333.29 g/mol. View Source

9. Molecular Biology Reports (2020) — Ashapkin V, Khavinson V, Shilovsky G, Linkova N, Vanuyshin B. Gene Expression in Human Mesenchymal Stem Cell Aging Cultures: Modulation by Short Peptides. AED peptide modulated IGF1, FOXO1, TERT, TNKS2, NFκB expression 1.6–5.6-fold. View Source

10. Advances in Gerontology (2014) — Khavinson VK, et al. Tripeptides Slow Down Aging Process in Renal Cell Culture. AED peptide decreased p16, p21, p53 while increasing SIRT6 in kidney epithelial cells. View Source

11. Biogerontology (2009) — Anisimov VN, Khavinson VK. Peptide Bioregulation of Aging: Results and Prospects. Long-term treatment with peptide preparations increased mean lifespan by 20–40% in animal models. View Source

12. Biochemistry (Moscow) (2015) — Ashapkin VV, Linkova NS, Khavinson VK, Vanyushin BF. Epigenetic Mechanisms of Peptidergic Regulation of Gene Expression during Aging of Human Cells. Demonstrates how short peptides regulate differentiation through epigenetic modulation. View Source

⚠️ Disclaimer: This page is provided for educational and informational purposes only and does not constitute medical advice, diagnosis, or treatment recommendations. Cartalax (AED peptide) is sold exclusively as a research compound, has not been approved by the FDA for any use, and is not intended for human consumption, self-administration, or any therapeutic application. All information is derived from published peer-reviewed literature. Research must comply with all applicable laws, regulations, and institutional guidelines.

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