Published · 10 references
MOTS-c vs NAD+
MOTS-c and NAD+ are different molecules: MOTS-c is a 16-residue peptide encoded within a ribosomal RNA gene, and NAD+ is a dinucleotide, not a peptide.
Structure at a glance
MOTS-c: C 101, N 28, O 22, S 2. NAD+: C 21, N 7, O 14, P 2.
Drawn from the product database. Each measure's bars share one scale.
| Property | MOTS-c | NAD+ |
|---|---|---|
| What it is | A 16-residue peptide encoded by a short open reading frame within the mitochondrial 12S rRNA gene.[1] Ends in a free C-terminal acid. | A dinucleotide, not a peptide.[2] Two nucleotide units joined through a pyrophosphate bridge. |
| How they relate | Different molecules. MOTS-c is encoded by a short open reading frame within the mitochondrial 12S rRNA gene.[1] NAD+ is a dinucleotide, not a peptide.[2] | |
| CAS number | 1627580-64-6 | 53-84-9 |
| Molecular formula | C101H152N28O22S2 | C21H27N7O14P2 |
| Molecular weight | 2,174.62 g/mol | 663.43 g/mol |
| Sequence | Met-Arg-Trp-Gln-Glu-Met-Gly-Tyr-Ile-Phe-Tyr-Pro-Arg-Lys-Leu-Arg | Not applicable (not a peptide) |
| Evidence base | Animal and cell studies. No completed controlled study testing MOTS-c in people has published results. Human studies in the literature reviewed for it measured the body's own MOTS-c. | Human studies of NAD+ itself, in the literature reviewed for it, include one randomized trial.[3] The trial, in one indication, was single-center and unreplicated, and used a surrogate endpoint.[3] |
| Regulatory status | MOTS-c is not approved for human therapeutic use, and Drugs@FDA holds no approved application for it.[4] | NAD+ holds no FDA approval.[5] |
| Compared head-to-head? | No direct comparison found in PubMed (searched October 2026).[6] | |
| Handling difference | MOTS-c has three oxidation-prone residues: two methionines and a tryptophan. NAD+ has two structural weak points that fail under opposite conditions: acid cleaves its pyrophosphate bridge, and alkaline conditions cleave its nicotinamide-ribose bond. | |
How MOTS-c and NAD+ differ
MOTS-c and NAD+ are different molecules. MOTS-c is a 16-residue peptide encoded by a short open reading frame within the mitochondrial 12S rRNA (ribosomal RNA) gene.[1] Its chain ends in a free C-terminal acid. NAD+ is nicotinamide adenine dinucleotide, a dinucleotide rather than a peptide.[2] It consists of two nucleotide units joined through a pyrophosphate bridge. The plus sign in its name denotes a permanent positive charge on the nitrogen of its nicotinamide ring.
No completed controlled study testing MOTS-c in people has published results. In the literature reviewed for MOTS-c, the human studies measured the body's own MOTS-c. The findings of the 2015 paper that first described MOTS-c are animal and cell findings, and none of them has been shown in humans.[1] In the literature reviewed for NAD+, a much larger body of work concerns two precursors, nicotinamide riboside and nicotinamide mononucleotide.[7][8] The two precursors are chemically distinct from NAD+, so a trial of either is not evidence about NAD+.[7][8]
In the literature reviewed for NAD+, the human studies of NAD+ itself are one randomized trial, one pharmacokinetic pilot and one retrospective record review.[3][9][10] The trial, in one indication, was single-center and has not been replicated.[3] Its primary endpoint was a surrogate imaging measure rather than a hard clinical outcome.[3] The pilot had three controls, and it reported no clinical outcome.[9] It was partly funded by a business with a commercial interest in NAD+ and run at a clinic with the same interest, and one author held roles at both.[9] The review was written by employees of a company with a commercial interest in NAD+, whose records it reviewed.[10]
MOTS-c is not approved for human therapeutic use, and Drugs@FDA holds no approved application for it.[4] NAD+ holds no FDA approval.[5]
MOTS-c carries two methionines and a tryptophan, three residues that can each take up oxygen when exposed to air, light or trace metals. A glutamine gives it a second, slower route, deamidation in solution. NAD+ has two structural weak points, and they fail under opposite conditions. Acid cleaves its pyrophosphate bridge into two mononucleotide halves. Alkaline conditions instead cleave the glycosidic bond that holds its nicotinamide to a ribose.
Have MOTS-c and NAD+ been compared directly?
No direct comparison of MOTS-c with NAD+ was found in a PubMed search run in October 2026.[6] That search covers PubMed only.
Read more on each compound
MOTS-c
Frequently Asked Questions
Is MOTS-c the same as NAD+?+−
MOTS-c and NAD+ are different molecules: MOTS-c is a 16-residue peptide encoded within a ribosomal RNA gene, and NAD+ is a dinucleotide, not a peptide. NAD+ consists of two nucleotide units joined through a pyrophosphate bridge.
References
- 2PubChem Compound records, NCBI (PUG-REST), for NAD+, NADH and NADP.
- 4US Food and Drug Administration. openFDA drug/label and drug/drugsfda endpoints, snapshot last updated 2026-08-26. Field-qualified substance-name query returned no record for MOTS-c.
- 5US FDA, openFDA drug/label and drug/drugsfda endpoints. Snapshot last updated 2026-08-26.
- 6PubMed search via NCBI E-utilities, run 3 October 2026; records entered to 2 October 2026. Query: ("MOTS-c"[tiab] OR "MOTSc"[tiab] OR "MOTS c"[tiab]) AND ("NAD+"[tiab] OR "NAD"[tiab] OR "nicotinamide adenine dinucleotide"[tiab] OR "nadide"[tiab]) AND ("1800/01/01"[edat] : "2026/10/02"[edat]). 2 records; none was a direct comparison of the two compounds.
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