MOTS-c vs NAD+: How the Two Compounds Compare in the Research
MOTS-c and NAD+ are two distinct research compounds that both appear in cellular-metabolism and mitochondrial-biology literature, and are frequently searched and catalogued together. This page compares their verified chemical identity and the preclinical research models in which each appears. It does not compare human outcomes and does not recommend either compound for any use; both are supplied strictly as research materials.
This comparison spans two different chemical classes: MOTS-c is a 16-residue mitochondrial-derived peptide, while NAD+ (nicotinamide adenine dinucleotide) is a dinucleotide coenzyme, not a peptide. The comparison is of verified chemical identity and the metabolic research models each appears in.
MOTS-c (Mitochondrial ORF of the Twelve-S rRNA type-c) is a 16-amino-acid peptide (sequence MRWQEMGYIFYPRKLR) that belongs to the class of mitochondrial-derived peptides (MDPs). It is unusual in that its sequence is encoded within the 12S rRNA region of mitochondrial DNA rather than nuclear DNA. In preclinical literature it is studied as a tool compound in metabolic-regulation and mitochondrial-signaling research models.
NAD+ (nicotinamide adenine dinucleotide) is not a peptide; it is a dinucleotide coenzyme composed of two nucleosides joined by a pyrophosphate bridge. It is one of the most fundamental coenzymes in cellular metabolism, functioning as an electron carrier in redox (oxidation-reduction) reactions and serving as a substrate in NAD+-dependent enzyme research. It is studied across a very broad preclinical literature in energy-metabolism and cellular-signaling models.
The two are therefore different classes of molecule (a mitochondrial-derived peptide versus a small-molecule coenzyme) that intersect in mitochondrial and metabolic research.
Side-by-side comparison (verified research properties)
| Property | MOTS-c | NAD+ (Nicotinamide adenine dinucleotide) |
|---|---|---|
| Compound class | Mitochondrial-derived peptide (MDP), 16 residues | Dinucleotide coenzyme (not a peptide) |
| CAS number | 1627580-64-6 | 53-84-9 |
| PubChem CID | 146675088 | 925 |
| Molecular formula | C101H152N28O22S2 | C21H27N7O14P2 (free acid form) |
| Molecular weight | ~2174.6 g/mol | ~663.4 g/mol (free acid) |
| Structure | 16-residue peptide; sequence MRWQEMGYIFYPRKLR | Two nucleosides joined by a pyrophosphate bridge |
| Genetic origin | Encoded within mitochondrial 12S rRNA DNA | Not gene-encoded; a metabolic coenzyme |
| Primary research models | Metabolic regulation, mitochondrial signaling (animal / cell models) | Redox reactions, NAD+-dependent enzyme studies, energy-metabolism models |
| Physical form | Lyophilized powder | Lyophilized powder / crystalline |
Data verified against PubChem (CID 146675088 and 925) and corroborating references. NAD+ is reported in multiple ionic/redox forms; the free-acid molecular weight is shown here.
How they differ in the research
The two compounds belong to fundamentally different chemical classes and are studied through different lenses:
- Class of molecule. MOTS-c is a 16-residue peptide; NAD+ is a small-molecule dinucleotide coenzyme. They are not chemically related and share no structural homology.
- Origin. MOTS-c is unusual among research peptides in that its sequence is encoded within mitochondrial DNA (the 12S rRNA region). NAD+ is not gene-encoded at all; it is a coenzyme synthesized through cellular metabolic pathways.
- Research-model role. MOTS-c is studied as a signaling peptide in metabolic-regulation and mitochondrial research models. NAD+ is studied for its role as an electron carrier in redox reactions and as a substrate/cofactor in NAD+-dependent enzyme research.
- Size. MOTS-c (~2174.6 g/mol) is substantially larger than NAD+ (~663.4 g/mol).
- Why they are paired. Both intersect in mitochondrial and energy-metabolism research, which is why they are frequently catalogued and studied together and are sometimes offered as a combined research blend. Any association is in the research models studied, not in established human effects.
Both compounds are described here only by their chemical identity and research-model context. Neither is an FDA-approved drug, and there are no controlled human trials establishing either for any use.
Frequently Asked Questions
What is the difference between MOTS-c and NAD+?
MOTS-c is a 16-amino-acid mitochondrial-derived peptide (MRWQEMGYIFYPRKLR, ~2174.6 g/mol) encoded within mitochondrial DNA and studied in metabolic-regulation research models. NAD+ is a dinucleotide coenzyme (~663.4 g/mol), not a peptide, studied as an electron carrier in redox reactions and as a cofactor in NAD+-dependent enzyme research. They belong to different chemical classes and share no structural homology.
Are MOTS-c and NAD+ the same kind of compound?
No. MOTS-c is a peptide; NAD+ is a small-molecule coenzyme. They are different chemical classes that intersect in mitochondrial and metabolic research literature but are structurally unrelated.
Are MOTS-c and NAD+ studied together?
They are frequently catalogued and studied together because both appear in mitochondrial and energy-metabolism research models, and they are sometimes offered as a combined research blend. Any association is within research-model contexts only; neither is approved for human use.
Is NAD+ a peptide like MOTS-c?
No. NAD+ (nicotinamide adenine dinucleotide) is a dinucleotide coenzyme composed of two nucleosides joined by a pyrophosphate bridge, not a peptide. MOTS-c is a 16-residue peptide.
Are MOTS-c or NAD+ approved for human use?
No. Neither MOTS-c nor NAD+ is an FDA-approved drug, and neither is intended for human consumption. Both are offered strictly as research compounds for laboratory use.
For research use only. Not for human or veterinary use. Not approved by the FDA. 21+
- HPLC + MS tested, every batch
- U.S. synthesized
- Batch COA on the product page
