MOTS-c kaufen in Europa

MOTS-c stands for mitochondrial open reading frame of the 12S rRNA type-c. It is a 16-amino-acid peptide with the sequence MRWQEMGYIFYPRKLR. What makes it structurally unusual among research peptides is where its coding sequence sits: not in the nuclear genome, but inside MT-RNR1, the mitochondrial gene for the 12S ribosomal RNA. It belongs to a small group of molecules described as mitochondrial-derived peptides (MDPs), a group that also includes humanin and the SHLP series. The peptide was characterised in a 2015 report in Cell Metabolism from Changhan Lee and colleagues at the University of Southern California (Lee et al., 2015).

The molecular formula is C101H152N28O22S2 and the molecular weight of the free peptide is 2174.62 g/mol (CAS 1627580-64-6). The two sulfur atoms come from methionine residues at positions 1 and 6. The sequence also contains a single tryptophan at position 3, two tyrosines, a proline at position 12, and four basic residues (three arginines and one lysine), which give the molecule a strongly cationic character at neutral pH. Those methionine and tryptophan residues are the chemically labile points of the molecule and the reason oxidising conditions and prolonged light exposure are avoided during handling.

Material supplied for laboratory work is produced by solid-phase peptide synthesis and lyophilised. Synthetic peptides of this class are commonly isolated as an acetate or trifluoroacetate salt, and the counter-ion adds mass beyond the 2174.62 g/mol free-peptide figure. This is worth noting because catalogue listings for the trifluoroacetate form give a formula weight of about 2288.6 for C101H152N28O22S2 combined with CF3COOH (Cayman Chemical item 29785), so a higher mass quoted by a supplier usually indicates the salt rather than a different molecule. PubChem indexes the trifluoroacetate form under the same compound record. Sequence conservation has been noted as a feature of the peptide: a review by Mohtashami and colleagues reports that the first 11 residues are highly conserved across 14 mammalian species (Mohtashami et al., 2022).

The founding paper is Lee et al., Cell Metabolism, 2015. It reported the identification of the short open reading frame within the mitochondrial 12S rRNA and characterised the resulting peptide. Mechanistically, the authors reported that MOTS-c inhibits the folate cycle and its tethered de novo purine biosynthesis, causing accumulation of AICAR and consequent activation of AMPK, and that its primary target organ appears to be skeletal muscle. In the animal arm of that work, the authors reported that MOTS-c treatment in mice prevented age-dependent and high-fat-diet-induced insulin resistance, and diet-induced obesity (Lee et al., 2015). These were mouse and cell-culture experiments.

A follow-up study from the same laboratory examined subcellular localisation. Kim, Son, Benayoun and Lee reported in Cell Metabolism (2018) that MOTS-c translocates to the nucleus and regulates nuclear gene expression following metabolic stress, in an AMPK-dependent manner, and that under glucose restriction it regulated a broad range of genes including those carrying antioxidant response elements. The authors also reported an interaction with the stress-responsive transcription factor NFE2L2/NRF2. Their framing was that the mitochondrial and nuclear genomes co-evolved to encode factors that cross-regulate each other (Kim et al., 2018).

The exercise literature is the second substantial thread. Reynolds et al., Nature Communications (2021), reported that in humans, exercise induced endogenous MOTS-c expression in skeletal muscle and in circulation. The interventional portion of that study was carried out in mice at three ages (2, 12 and 22 months), where the authors reported enhanced physical performance following MOTS-c administration, along with changes in nuclear gene expression, skeletal muscle metabolism, and myoblast adaptation to metabolic stress. The paper also described a late-life protocol, in which mice were transitioned to intermittent treatment three times per week at 23.5 months of age (Reynolds et al., 2021).

Human evidence to date is observational and genetic rather than interventional. Ramanjaneya et al., Frontiers in Endocrinology (2019), measured circulating mitochondrial-derived peptides across 225 subjects (68 normoglycaemic, 33 prediabetic, 31 with well-controlled type 2 diabetes, and 93 with poorly controlled type 2 diabetes) and reported that serum MOTS-c concentrations were significantly lower in the poorly controlled type 2 diabetes group than in healthy controls, and that circulating MOTS-c correlated negatively with age, HbA1c and glucose. That study was cross-sectional and observational, not an intervention. Separately, Zempo et al., Aging (2021), described an Asian-specific mitochondrial DNA variant, m.1382A>C (rs111033358), which produces a K14Q amino-acid substitution in the peptide; the authors reported an association between this polymorphism and type 2 diabetes susceptibility in men in the cohorts they examined.

No peer-reviewed interventional trial of native MOTS-c in humans could be confirmed at the time of writing. Two registry entries are relevant. CB4211, described by its sponsor CohBar as an analogue of MOTS-c and not the native peptide, completed a phase 1a/1b trial in healthy non-obese subjects and subjects with non-alcoholic fatty liver disease (NCT03998514; 88 participants enrolled; completed April 2021); no peer-reviewed publication of those results could be located. A phase 2a study of MOTS-c itself in adults with prediabetes and overweight or obesity was first posted in April 2026 (NCT07505745; sponsor Hudson Biotech; 120 participants planned; co-primary endpoints the change from baseline in the OGTT-derived Matsuda index at 12 weeks and the incidence of treatment-emergent adverse events at 16 weeks) and is listed as recruiting, with no results posted. Beyond those registry records, the published record for this compound remains preclinical.

Reviews covering the field include Wan et al., Journal of Translational Medicine (2023), which summarises the stress, metabolic and ageing literature and describes the folate-AICAR-AMPK route as the principal proposed mechanism.