5-Amino-1MQ vs MOTS-c
5-Amino-1MQ (Small-molecule NNMT inhibitor) 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 | 5-Amino-1MQ | MOTS-c |
|---|---|---|
| Compound class | Small-molecule NNMT inhibitor | Mitochondrial-derived peptide |
| Research category | Metabolic & Mitochondrial | Metabolic & Mitochondrial |
| Length (amino acids) | Not documented | 16 amino acids |
| Molecular weight | ~159 g/mol (free base) | ~2174 g/mol |
| Half-life | Not documented | Not documented |
| Origin | 5-Amino-1-methylquinolinium (5-Amino-1MQ) is a synthetic small-molecule quinolinium compound. It is not a peptide. It was identified as a cell-permeable inhibitor of the enzyme nicotinamide N-methyltransferase (NNMT). | 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 5-Amino-1MQ works
5-Amino-1MQ inhibits NNMT, the enzyme that methylates nicotinamide using S-adenosylmethionine. By inhibiting NNMT, it is proposed to preserve cellular nicotinamide and NAD+ pools and reduce a metabolic sink associated with adipocyte expansion. In preclinical rodent studies, NNMT inhibition has been associated with reduced adipose tissue mass and altered cellular energy metabolism.
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.
5-Amino-1MQ
MOTS-c
What sets each apart
5-Amino-1MQ
Distinct from the peptides in this group: it is an orally-oriented small-molecule enzyme inhibitor acting on NNMT, rather than a receptor- or fragment-based peptide.
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
Is 5-Amino-1MQ a peptide?
No. 5-Amino-1MQ is a small-molecule NNMT inhibitor, chemically a methylquinolinium (5-amino-1-methylquinolinium) compound. It is often grouped with metabolic peptides in catalogs because of its fat-metabolism research context, but structurally it is a small molecule, not a peptide, and has no amino-acid sequence.
What is the mechanism of 5-Amino-1MQ?
5-Amino-1MQ competitively inhibits nicotinamide N-methyltransferase (NNMT) at its catalytic site. NNMT consumes S-adenosylmethionine (SAM) and methylates nicotinamide; inhibiting it is reported to raise intracellular SAM and NAD+ availability in adipocytes, shifting cells toward a more metabolically active, fat-oxidizing phenotype in preclinical models.
What is 5-Amino-1MQ studied for?
It is studied primarily in models of obesity and adipose-tissue metabolism, where NNMT is highly expressed in white/visceral fat. Preclinical rodent work reported reductions in body weight and fat mass with NNMT inhibition. Human clinical data remain limited, so findings are preclinical/mechanistic in nature.
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.