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Compound Overviews

Who Discovered MOTS-c? The Mitochondrial-Derived Peptide

3 min read · Updated 2026-06-01 · VaultLabs Research Editorial · Reviewed by VaultLabs compliance review

How MOTS-c was identified, why it is encoded in mitochondrial rather than nuclear DNA, and what the metabolic literature reports. Research use only.

Research use only. For in vitro research use only. Not for human or animal consumption. Not for human consumption, medical use, or personal application.

A peptide encoded by the mitochondrion

MOTS-c is unusual among research peptides because of where its gene sits. It is encoded within the mitochondrial 12S ribosomal RNA gene rather than in nuclear DNA — a short open reading frame inside a sequence that was long assumed to code for nothing.

The peptide was identified by Changhan David Lee and colleagues, working with Pinchas Cohen's group, and reported in Cell Metabolism in 2015. That paper described the sequence, its mitochondrial origin, and the metabolic effects observed in mouse models.

The name reflects the finding: mitochondrial open reading frame of the twelve S rRNA type-c. The literature spelling is MOTS-c; some catalogues, including this one, shorten it to MOT-C, and both refer to the same sequence.

For research and laboratory use only. Not for human consumption, medical use, or personal application.

What the research covers

Published work concentrates on metabolic endpoints in cell and rodent systems — AMPK pathway activation, glucose handling, and effects described in the exercise-physiology literature. Lee and colleagues followed the discovery paper with further characterisation in Free Radical Biology and Medicine in 2016.

Reviews since then have surveyed the wider mitochondrial-derived peptide family. Zheng and colleagues published a review in Frontiers in Endocrinology in 2023 covering the signalling work, and Benayoun and Lee described the peptide's regulatory relationship with the nucleus in BioEssays in 2019.

This is a young literature by comparison with the copper peptides. The discovery paper is from 2015, which means fewer independent replications and more results that have not yet been tested outside the originating group.

Analytical notes

Because the catalogue name and the literature name differ, incoming-goods documentation should record both. A certificate reading MOT-C and a purchase order reading MOTS-c refer to the same material, and the equivalence should be written down rather than assumed by whoever reads the file later.

The sequence contains no cysteine, so there is no disulfide bridge to preserve and no reduced-versus-oxidised ambiguity during mass confirmation. Standard reversed-phase methods for short peptides apply.

For research and laboratory use only. Not for human consumption, medical use, or personal application.

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