MOTS-c

MOTS-c is a 16-residue peptide encoded by the mitochondrial 12S rRNA region rather than by nuclear DNA, one of a small group of mitochondrial-derived peptides. It is supplied as a lyophilised solid. Identity is confirmed by mass spectrometry and purity by reversed-phase HPLC with a stated method. Because the sequence is short and its commercial supply recent, batch-to-batch identity confirmation is a more meaningful documentation check than a purity percentage alone. Analytical values on this record are transcribed from supplier documentation.

MOTS-c was described in 2015 by a research group studying short open reading frames within mitochondrial DNA, following earlier work on humanin. Its identification was significant conceptually because it supported the idea that the mitochondrial genome encodes signalling peptides that act beyond the organelle. The field is young: essentially the whole literature postdates 2015, and the number of independent groups working on it remains small.

Published work examines activation of AMP-activated protein kinase, effects on the folate-methionine cycle and on AICAR accumulation, regulation of glucose uptake in skeletal muscle preparations, and translocation to the nucleus under metabolic stress with reported effects on stress-response gene expression. Rodent studies examined insulin sensitivity, diet-induced obesity endpoints and exercise capacity. Human observational work has examined circulating peptide concentrations in relation to age and metabolic status.

Mitochondrial encoding of the peptide and its detectability in human plasma are established findings. AMPK activation in cell and rodent systems has been reported by more than one group. Association between lower circulating concentrations and older age or adverse metabolic status has been observed in more than one cohort, though association is not causation and the cohorts are small.

Independent confirmation that the peptide is translated and detectable, rather than being an artefact of sequence prediction, has come from more than one laboratory using mass-spectrometric detection in human samples. That is a meaningful baseline finding and should be distinguished from the functional claims built on top of it.

There are no completed randomised controlled human trials of administered MOTS-c for any indication. Every interventional finding is from cell culture or rodent models, and the rodent studies use small groups with short durations. The literature is concentrated in a small number of related laboratories, so apparent consistency across papers overstates the degree of independent replication. Human data are observational and cross-sectional, which cannot distinguish cause from consequence: lower concentrations in metabolically unwell participants may be a marker rather than a driver. Pharmacokinetics of exogenously supplied peptide in humans are unstudied. This is an early-stage research subject and should be evaluated as one.

Store the lyophilised solid per the storage conditions on this record, protected from light and moisture, with the sealed vial equilibrated before opening. Humidity uptake and repeated freeze-thaw of reconstituted material are the principal handling risks. This section describes laboratory handling of the material as supplied and provides no preparation or administration procedure.

Because the commercial supply of this peptide is recent and the analytical reference standards are less widely distributed than for older sequences, comparing certificates between suppliers is harder and identity confirmation on each batch is correspondingly more important.

Indexed citations with verified PMIDs appear below. See testing methodology for analytical methods and sourcing standards for batch documentation requirements. Related metabolic records are listed in the compound index.