Anti-Aging

Cartalax (Ala-Glu-Asp) is a synthetic tripeptide developed by Vladimir Khavinson at the St. Petersburg Institute of Bioregulation and Gerontology as part of the bioregulator peptide program. It belongs to a class of ultra-short peptides (2-4 amino acids) that Khavinson's group has investigated for tissue-specific regulatory effects over several decades. Cartalax was designed to target cartilage and musculoskeletal tissue, with the aim of preserving cartilage integrity and promoting chondrocyte function during aging. The bioregulator peptide concept posits that short peptides can interact directly with DNA through sequence-specific binding to the minor groove, influencing gene expression without requiring membrane receptor activation. This is a non-conventional mechanism for peptide action and remains an area of active research, primarily within Russian academic institutions. Cartalax is part of a larger family of Khavinson peptides that includes Epitalon (AEDG), Pinealon (EDR), and others, each claimed to have tissue-specific tropism.

Epitalon (also spelled Epithalon) is a synthetic tetrapeptide with the sequence Ala-Glu-Asp-Gly, developed by Professor Vladimir Khavinson at the St. Petersburg Institute of Bioregulation and Gerontology in Russia. It is the synthetic analogue of Epithalamin, a peptide extract derived from the bovine pineal gland that was studied for its anti-aging properties beginning in the 1980s. Epitalon was designed to reproduce the biological activity of Epithalamin in a defined, reproducible synthetic form. The primary research interest in Epitalon centers on its reported ability to activate telomerase, the enzyme responsible for maintaining telomere length at chromosome ends. Telomere shortening is a hallmark of cellular aging, and interventions that preserve telomere length have been hypothesized to extend cellular and organismal lifespan. While Epitalon research has generated intriguing in vitro and animal data, the evidence base consists primarily of studies from a single research group, and no large-scale clinical trials have been conducted outside of Russia.

GHK-Cu (glycyl-L-histidyl-L-lysine:copper(II)) is a naturally occurring copper-binding tripeptide first identified in human plasma in 1973 by Loren Pickart. It consists of three amino acids — glycine, histidine, and lysine — complexed with a copper(II) ion at a 1:1 ratio. The peptide is found in plasma, saliva, and urine, with circulating levels that decline significantly with age: from approximately 200 ng/mL at age 20 to roughly 80 ng/mL by age 60. GHK-Cu has attracted research interest for its unusually broad biological activity profile relative to its small size. It modulates the expression of over 4,000 human genes, representing roughly 6% of the genome, with a net effect that shifts gene expression patterns toward tissue repair, anti-inflammatory, and antioxidant states. It is commercially available in cosmetic formulations and remains under investigation for wound healing, tissue remodeling, and anti-aging applications.

SS-31 (elamipretide, formerly Bendavia/MTP-131) is a synthetic tetrapeptide that selectively targets the inner mitochondrial membrane. Developed by Hazel Szeto at Weill Cornell Medical College, it is the lead compound in a class of mitochondria-targeted peptides (Szeto-Schiller peptides) designed to restore mitochondrial function in aging and disease. The peptide carries a 3+ charge at physiological pH due to its D-arginine and lysine residues, which drives its rapid, energy-independent accumulation in mitochondria at concentrations 1,000-5,000 fold greater than in the cytoplasm. Elamipretide is in clinical development by Stealth BioTherapeutics for several mitochondrial diseases, including Barth syndrome, primary mitochondrial myopathy, and age-related macular degeneration. It represents a fundamentally different approach to antioxidant therapy — rather than scavenging reactive oxygen species after they form, SS-31 optimizes mitochondrial electron transport to prevent excessive ROS generation at the source. This mechanism has generated interest in the anti-aging research community, as mitochondrial dysfunction is a hallmark of cellular aging.