Humanin vs MOTS-c
Humanin (Mitochondrial-derived peptide) and MOTS-c (Mitochondrial-derived peptide) are documented as co-studied in the PeptiDex library. This page puts the two entries side by side on class, molecular weight, half-life, origin, mechanism and studied research areas — every value taken from the entry it belongs to.
Why these two are co-studied
Cross-referenced for research context — not a usage or combination recommendation.
At a glance
| Attribute | Humanin | MOTS-c |
|---|---|---|
| Compound class | Mitochondrial-derived peptide | Mitochondrial-derived peptide |
| Research category | Longevity & Cellular | Metabolic & Mitochondrial |
| Length (amino acids) | 24 amino acids | 16 amino acids |
| Molecular weight | 2687 g/mol (approx., 24-aa form) | ~2174 g/mol |
| Half-life | Not documented | Not documented |
| Origin | Humanin is a small mitochondrial-derived peptide encoded within the mitochondrial 16S ribosomal RNA gene (MT-RNR2). It was identified in the early 2000s from surviving neurons in Alzheimer's disease brain tissue and is one of the first characterized mitochondrial-derived peptides. | MOTS-c (Mitochondrial ORF of the 12S rRNA type-c) is a 16-amino-acid mitochondrial-derived peptide encoded within the MT-RNR1 (12S rRNA) region of mitochondrial DNA. It was described in 2015 and is one of a small family of mitochondrial-derived peptides. |
“Not documented” means the PeptiDex entry records no value for that field. Nothing on this page is estimated, and no figure is carried over from one compound to the other.
How Humanin works
Humanin is reported to have cytoprotective and anti-apoptotic effects. Described mechanisms include interaction with pro-apoptotic Bcl-2 family proteins (such as Bax and BID) and signaling through a cell-surface receptor complex, with downstream effects on cell survival pathways. It has also been studied for roles in metabolic regulation and insulin sensitivity. Both a 24-amino-acid form (mitochondrial translation) and a 21-amino-acid form (cytoplasmic translation) have been described.
How MOTS-c works
MOTS-c is reported to regulate metabolic homeostasis, in part via activation of the AMPK pathway and modulation of the folate-methionine cycle and de novo purine biosynthesis. It has been described to translocate to the nucleus under metabolic stress and influence stress-response gene expression. Preclinical work links it to improved insulin sensitivity and glucose uptake in skeletal muscle; it is also described as exercise-responsive.
Mechanistic descriptions reflect published research-literature understanding and are quoted from each compound's own entry. Much peptide research is preclinical (in-vitro or animal-model); mechanism in humans may differ and is not established for many compounds.
Where each one appears in the literature
The research contexts each entry documents. Listing a research area is not a claim of efficacy or a therapeutic indication, and the two lists are not scored against each other.
Humanin
MOTS-c
What sets each apart
Humanin
Humanin is a naturally encoded mitochondrial-derived signaling peptide focused on cytoprotection and metabolism, distinct from the synthetic mitochondria-targeting SS-31 and from immune or pineal peptides.
MOTS-c
Unlike the GH-derived fragments here, MOTS-c is endogenously encoded in the mitochondrial genome and acts as a broad metabolic regulator rather than a targeted lipolytic fragment.
Frequently asked questions
What is humanin?
Humanin is a 24-amino-acid mitochondrial-derived peptide (MDP) encoded within the 16S rRNA region of mitochondrial DNA, discovered in 2001. It is the founding member of the mitochondrial-derived peptide family and is studied for cytoprotective, neuroprotective, and metabolic effects.
What is the sequence and molecular weight of humanin?
Humanin's sequence is MAPRGFSCLLLLTSEIDLPVKRRA, a 24-residue peptide with an approximate molecular weight of about 2687 Da. Some research analogs (e.g. HNG, with a Ser14Gly substitution) are more potent variants used in studies.
What is humanin studied for?
Preclinical research has examined humanin for neuroprotection against amyloid-beta toxicity, cardioprotection in ischemia-reperfusion injury, insulin sensitization via central STAT3 signaling, and anti-apoptotic effects through BAX antagonism. These are cell and animal findings, not established human therapies.
What is MOTS-c and where does it come from?
MOTS-c (Mitochondrial Open-reading-frame of the Twelve-S rRNA type-c) is a 16-amino-acid mitochondrial-derived peptide (MDP) encoded within the 12S rRNA region of mitochondrial DNA, rather than by the nuclear genome. First described in 2015, it is studied as a regulator of metabolic homeostasis. Its sequence and MDP origin make it structurally distinct from most catalog peptides.
What is MOTS-c studied for?
MOTS-c is studied in models of metabolic homeostasis, insulin sensitivity, exercise capacity, and aging. Research reported that MOTS-c levels rise with exercise and that exogenous MOTS-c improved glucose tolerance, insulin sensitivity, and running endurance in aged mice. It is thought to act partly via AMPK-linked metabolic signaling.
How is MOTS-c thought to work mechanistically?
MOTS-c is reported to translocate to the nucleus under metabolic stress and influence adaptive gene-expression programs, and it engages the AMPK pathway and folate/one-carbon metabolism to promote glucose uptake and fatty-acid oxidation. This positions it as a signaling peptide linking mitochondrial state to whole-body metabolism in preclinical models.
Answers are the ones published on each compound's own PeptiDex entry. They are educational summaries of research-literature context and are not medical advice.