Mitochondrial peptides: SS-31, MOTS-c and NAD+ as three distinct literature areas

Last reviewed 9 August 2026

Three compounds are routinely shelved together under the word mitochondrial, and the grouping does real damage to anyone trying to read the evidence. SS-31 is a four-residue synthetic peptide. MOTS-c is a sixteen-residue peptide encoded by the mitochondrial genome itself. NAD+ is not a peptide at all — it is a dinucleotide coenzyme. They share a subcellular compartment and very little else.

What follows keeps them apart. Each entry reports what a named study examined, in what model, and what its authors reported; no conclusion is drawn across the three. A fourth compound, 5-Amino-1MQ, is covered at the end, because it connects to the NAD+ section through an enzyme rather than a shared class.

Three different kinds of molecule

Two of the four have no amino-acid sequence, so assumptions carried over from peptide work do not automatically apply. Of the two that are peptides, one was drawn on a chemist’s bench and one is transcribed from a genome. Full identification data sits in the library entries for SS-31, MOTS-c, NAD+ and 5-Amino-1MQ.

SS-31 (elamipretide): a designed tetrapeptide and a cardiolipin literature

In vitro, isolated mitochondria and model membranes

Zhao and colleagues (2004) investigated a series of aromatic-cationic peptides in isolated mitochondria, neuronal N2A cell culture and an isolated perfused organ reperfusion model, and reported that the peptides concentrated in the inner mitochondrial membrane, lowered reactive oxygen species production and inhibited permeability transition and swelling in those systems. This is the foundational characterisation paper for the series. [1]

Birk and colleagues (2013) investigated the binding target in isolated mitochondria and a rat kidney ischaemia–reperfusion model, and reported high-affinity binding to cardiolipin — an anionic phospholipid of the inner mitochondrial membrane — and that the resulting complex inhibited the cytochrome c peroxidase activity catalysing cardiolipin peroxidation. [2] Mitchell and colleagues (2020) investigated the interaction in model lipid bilayers and in mitochondrial membranes isolated from yeast (Saccharomyces cerevisiae), including the Δtaz1 and Δcrd1 deletion strains, and reported that the peptide partitions into the membrane interfacial region with an affinity related to surface charge and altered the surface electrostatics of both. [3] Chavez and colleagues (2020) investigated which mitochondrial proteins the peptide contacts, by cross-linking and mass spectrometry in heart mitochondria from young and aged mice, and reported twelve cross-linked proteins, all known cardiolipin binders. [4]

A 2025 review by Sabbah and colleagues records how that account changed: the earliest descriptions were framed around reactive-oxygen-species scavenging, and cardiolipin binding and its membrane consequences are now central to how the authors describe the mechanism. [5]

Human studies

• Karaa and colleagues (2018) investigated the compound in a randomised, double-blind, placebo-controlled dose-escalation phase 1/2 study in 36 adults with genetically confirmed primary mitochondrial myopathy, and reported that the highest-dose group walked 64.5 m farther at day 5, the primary timepoint, against 20.4 m for placebo, a difference that did not reach significance (p = 0.053), with a graded relationship across the dose groups (p = 0.014). [6]
• Reid Thompson and colleagues (2021) investigated it in a randomised, double-blind, placebo-controlled crossover trial in 12 participants with Barth syndrome, a genetic disorder of mitochondrial cardiolipin metabolism, followed by an uncontrolled open-label extension. They reported that neither primary endpoint was met in the randomised part, and reported changes on both measures in the uncontrolled open-label extension (six-minute walk +95.9 m, p = 0.024; symptom assessment −2.1 points, p = 0.031). [7]
• Karaa and colleagues (2023) investigated it in MMPOWER-3, a randomised, double-blind, placebo-controlled trial in 218 adults with primary mitochondrial myopathy, and reported that the co-primary endpoints were not met: no significant difference against placebo on the six-minute walk test or the total fatigue score. This is the largest randomised trial of the compound published. [8]
• Karanjia and Sadun (2024) investigated it in a randomised, vehicle-controlled phase 2 trial in 12 participants with genetically confirmed Leber hereditary optic neuropathy, and reported that the primary efficacy endpoint was not met. The formulation studied differed from those used in the three trials above. [9]

Regulatory record

The FDA granted accelerated approval to elamipretide, as Forzinity, on 19 September 2025, to improve muscle strength in adult and paediatric patients with Barth syndrome weighing at least 30 kg. [10] [11] Two features of that decision bear on reading the literature: the approval rests on an improvement in knee extensor muscle strength, which the FDA designates an intermediate clinical endpoint — a clinical measurement taken earlier than the outcomes of interest and regarded as reasonably likely to predict them, rather than a demonstration of those outcomes — and continued approval may be contingent on verification of clinical benefit in a confirmatory trial. [10] It covers that indication in one rare inherited condition and nothing else. No UK marketing authorisation was identified. The EMA granted orphan designation for Barth syndrome (EU/3/21/2430) on 20 May 2021, a development status rather than an authorisation to market. [12] A registered phase 2a study in healthy ageing and physical function is recruiting; it is open-label and single-arm, so it carries no control group, and no results are published. [13]

MOTS-c: a peptide the mitochondrial genome encodes

MOTS-c belongs to a defined class. Hashimoto and colleagues (2001) identified humanin, a short polypeptide, by functional expression screening in neuronal cell models. [14] Its origin in a short open reading frame of mitochondrial DNA is established in the later literature rather than in that paper. [15] [16] Cobb and colleagues (2016) characterised six further peptides encoded in the mitochondrial 16S rRNA region — the small humanin-like peptides — in cell culture and in rodents. [15] A 2024 review by Kal and colleagues groups all three sets as products of short open reading frames in mitochondrial DNA. [16]

In vitro and rodent models

Lee and colleagues (2015) investigated a peptide product predicted from a short open reading frame within the mitochondrial 12S rRNA, in human and rodent cell lines and in mice, and reported the identification of that reading frame and its peptide product, effects on the metabolic parameters they measured in mouse models including diet-induced obesity, and a proposed mechanism running through the folate pathway, de novo purine biosynthesis and AMPK activation. [17]

Kim, Son, Benayoun and Lee (2018) investigated subcellular localisation under metabolic stress in cell models, and reported translocation of the peptide to the nucleus in an AMPK-dependent manner and interaction with stress-responsive transcription factors at antioxidant response elements. [18] Reynolds and colleagues (2021) administered MOTS-c to young, middle-aged and old mice (2, 12 and 22 months), and to a further group from 23.5 months, and reported that those mice recorded higher values on the physical capacity measures used; in an accompanying human component the authors measured endogenous expression and reported that it rose in skeletal muscle and in circulation after exercise. [19]

Human studies

This is where the MOTS-c literature is most often misread. A PubMed search on 9 August 2026 for "MOTS-c"[Title/Abstract] returned 246 records, four of them typed as randomised controlled trials. In all four, MOTS-c is a measured biomarker and something else is the intervention.

• Elhusseiny and colleagues (2025) — the intervention was repeated heat stress during calf immobilisation in 19 physically active men; circulating MOTS-c was an outcome measured. [20]
• Dieli-Conwright and colleagues (2021) — the intervention was a 16-week aerobic and resistance exercise programme; plasma MOTS-c was measured by ELISA. [21]
• von Walden and colleagues (2021) — the intervention was a single bout of endurance or resistance exercise; circulating mitochondrial-derived peptides were measured before and after. [22]
• Cuyàs and colleagues, for the METTEN study group (2022) — the intervention was metformin added to neoadjuvant therapy; MOTS-c was measured in paired sera, and the authors reported no significant alteration. [23]

No published study in which MOTS-c itself was administered to human participants was identified. One registered interventional study is now under way: NCT07505745, a randomised, double-blind, placebo-controlled phase 2a study in adults with prediabetes and overweight or obesity, sponsored by Hudson Biotech, estimated enrolment 120, started 2 February 2026, estimated primary completion February 2027. Its primary outcomes are a change from baseline in an insulin-sensitivity index derived from a glucose tolerance test, and the incidence of adverse events arising during the study. No results are published. [24]

NAD+: a cofactor, and a literature that is mostly about its precursors

Covarrubias, Perrone, Grozio and Verdin (2021) reviewed NAD+ metabolism across in vitro, animal and human literature, describing NAD+ as both a redox coenzyme and a substrate for sirtuins and PARPs, with tissue concentrations declining with age across several models. [25]

The distinction that governs how the human literature can be read is biochemical rather than pedantic. Nikiforov, Dölle, Niere and Ziegler (2011) investigated how extracellular precursors reach the intracellular NAD pool, in cultured human 293, HeLa S3 and HepG2 cells using a targeted PARP1 catalytic domain as a sensor, and reported that the nucleosides readily enter cells while the larger nucleotides are broken down extracellularly first — NAD itself had to be degraded to nicotinamide riboside before it could serve as a precursor of intracellular NAD+. [26]

That is why a trial of a precursor is a trial of a different molecule. A PubMed search on 9 August 2026 returned 31 records typed as randomised controlled trials for "nicotinamide riboside"[Title/Abstract] and 16 for "nicotinamide mononucleotide"[Title/Abstract]. The three usually cited here are among them, and in each the intervention was the precursor:

• Martens and colleagues (2018), a randomised, double-blind, placebo-controlled crossover trial in 24 healthy middle-aged and older adults, reported that nicotinamide riboside was tolerated and that blood NAD+ was elevated relative to placebo. [27]
• Elhassan and colleagues (2019), a randomised, double-blind, placebo-controlled crossover trial in 12 aged men with skeletal muscle biopsy, reported augmentation of the muscle NAD+ metabolome together with transcriptomic signatures the authors characterised as anti-inflammatory. [28]
• Brakedal and colleagues (2022), a double-blind randomised phase 1 trial in 30 newly diagnosed participants with Parkinson’s disease, reported tolerability and measurable changes in cerebral NAD. [29]

Published human work on the intact dinucleotide is thin by comparison: Grant and colleagues (2019) reported a pilot study in 11 participants, 8 receiving NAD+ and 3 controls, characterising the plasma and urine NAD+ metabolome during administration. [30] An evidence claim about NAD+ resting on a nicotinamide riboside trial is resting on a different compound taking a different path into the cell.

5-Amino-1MQ and NNMT: the same pathway, a different kind of molecule

Nicotinamide N-methyltransferase transfers a methyl group from S-adenosylmethionine to nicotinamide, producing 1-methylnicotinamide and consuming nicotinamide — a precursor of NAD+. The connection is enzymatic rather than structural; a 2024 review by Sun and colleagues sets out the pathway in those terms. [31] Neelakantan and colleagues (2018) investigated small-molecule NNMT inhibitors of the quinolinium series in adipocytes and in diet-induced obese C57BL/6 mice, and reported increased intracellular NAD+ and S-adenosylmethionine in adipocytes, and reduced body weight, white adipose mass, adipocyte size and plasma total cholesterol in the mice receiving the inhibitor relative to controls, without a change in food intake. [32]

The designation deserves a note of its own. A PubMed search on 9 August 2026 for "5-amino-1MQ" returned zero records; the chemical name "5-amino-1-methylquinolinium" returned three. A search for "nicotinamide N-methyltransferase" AND inhibitor, filtered to the randomised controlled trial publication type, returned zero. The name this compound is sold under is not the name its literature is indexed under — a practical obstacle to checking any claim made about it.

What the 2026 Prohibited List says

Read against the World Anti-Doping Agency’s 2026 Prohibited List, including its index, the four compounds are not in the same position.

• MOTS-c is named. It appears at S4.4.1, under Metabolic Modulators, in the entry Activators of the AMP-activated protein kinase (AMPK), e.g. 5-N,6-N-bis(2-fluorophenyl)-[1,2,5]oxadiazolo[3,4-b]pyrazine-5,6-diamine (BAM15), AICAR, mitochondrial open reading frame of the 12S rRNA-c (MOTS-c). Substances in class S4.4 are non-Specified, and S4 is prohibited at all times. [33]
• Elamipretide, SS-31, nicotinamide adenine dinucleotide and NNMT inhibitors are not named anywhere on the List. S0 covers Any pharmacological substance which is not addressed by any of the subsequent sections of the List and with no current approval by any governmental regulatory health authority for human therapeutic use. [33]

Whether S0 reaches a particular substance turns on approval facts that change over time, and it is a question for an athlete’s anti-doping organisation. The current List is the operative document and this page publishes no interpretation of it.

Four places these literatures get crossed

1. A nicotinamide riboside trial cited as NAD+ evidence. The molecule administered was the precursor, and the cell-biology work gives a specific reason why the two are not interchangeable. [26]
2. An exercise study cited as MOTS-c evidence. Every randomised controlled trial indexed against the term measured MOTS-c as an outcome of some other intervention. [20] [21] [22] [23]
3. A regulatory approval read beyond its scope. The elamipretide approval is accelerated, limited to muscle strength in patients above a weight threshold within one rare inherited condition, on an intermediate clinical endpoint, with a confirmatory trial required — and the largest published randomised trial of the same molecule did not meet its co-primary endpoints. [8] [10]
4. Two of the four described as peptides. NAD+ and 5-Amino-1MQ have no amino-acid sequence.

What the four do have in common

Handling arithmetic, and little else. Concentration after reconstitution is the mass of lyophilised solid divided by the volume of diluent added, and that relation is indifferent to which compound is in the vial and to whether the diluent is preserved. The reconstitution calculator resolves it and its vial presets fill in strength only; the method is set out in how to calculate peptide concentration after reconstitution.

Stability diverges again, chemically. MOTS-c carries two methionine residues and one tryptophan, among the most oxidation-prone residues in peptide chemistry; SS-31 carries neither, and its oxidation-sensitive feature is the phenolic dimethyltyrosine; NAD+ is not a peptide at all, and its solution instability is pH-dependent in the opposite direction to that of its reduced form. Each is set out in the storage section of the relevant library entry. The four sit together in the Longevity & Cellular category for catalogue reasons, not evidentiary ones; how the grades on those entries are assigned is described in how evidence grades work on this site.

References

Where a publication’s own title states a route, a formulation or an administered amount, or is itself written in claim register, the title is omitted from the citation line and the record is identified by its PMID instead. The model is named in every line.

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2. Birk AV, Liu S, Soong Y, Mills W, Singh P, Warren JD, Seshan SV, Pardee JD, Szeto HH. The mitochondrial-targeted compound SS-31 re-energizes ischemic mitochondria by interacting with cardiolipin. J Am Soc Nephrol. 2013;24(8):1250–61. Model: isolated mitochondria and rat ischaemia–reperfusion. PMID 23813215 · doi:10.1681/ASN.2012121216
3. Mitchell W, Ng EA, Tamucci JD, Boyd KJ, Sathappa M, Coscia A, Pan M, Han X, Eddy NA, May ER, Szeto HH, Alder NN. The mitochondria-targeted peptide SS-31 binds lipid bilayers and modulates surface electrostatics as a key component of its mechanism of action. J Biol Chem. 2020;295(21):7452–69. Model: in vitro, model membranes and mitochondria isolated from yeast (Saccharomyces cerevisiae), including the Δtaz1 and Δcrd1 deletion strains. PMID 32273339 · doi:10.1074/jbc.RA119.012094
4. Chavez JD, Tang X, Campbell MD, et al. Mitochondrial protein interaction landscape of SS-31. Proc Natl Acad Sci U S A. 2020;117(26):15363–73. Model: ex vivo, heart mitochondria isolated from young and aged mice. PMID 32554501 · doi:10.1073/pnas.2002250117
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7. Reid Thompson W, Hornby B, Manuel R, Bradley E, Laux J, Carr J, Vernon HJ. A phase 2/3 randomized clinical trial followed by an open-label extension to evaluate the effectiveness of elamipretide in Barth syndrome, a genetic disorder of mitochondrial cardiolipin metabolism. Genet Med. 2021;23(3):471–8. Model: human — randomised, double-blind, placebo-controlled crossover, n = 12, plus uncontrolled open-label extension. PMID 33077895 · doi:10.1038/s41436-020-01006-8
8. Karaa A, et al. Efficacy and Safety of Elamipretide in Individuals With Primary Mitochondrial Myopathy: The MMPOWER-3 Randomized Clinical Trial. Neurology. 2023;101(3):e238–52. Model: human — randomised, double-blind, placebo-controlled trial, n = 218. PMID 37268435 · doi:10.1212/WNL.0000000000207402
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13. ClinicalTrials.gov, NCT07275424. Study of Healthy Aging and Physical Function With Elamipretide. Open-label, single-arm phase 2a pilot study; sponsor University of Washington; recruiting; no published results. Model: trial registry record. clinicaltrials.gov
14. Hashimoto Y, Niikura T, Tajima H, Yasukawa T, Sudo H, Ito Y, Kita Y, Kawasumi M, Kouyama K, Doyu M, Sobue G, Koide T, Tsuji S, Lang J, Kurokawa K, Nishimoto I. A rescue factor abolishing neuronal cell death by a wide spectrum of familial Alzheimer’s disease genes and Aβ. Proc Natl Acad Sci U S A. 2001;98(11):6336–41. Model: in vitro, neuronal cell models. PMID 11371646 · doi:10.1073/pnas.101133498
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17. Lee C, Zeng J, Drew BG, Sallam T, Martin-Montalvo A, Wan J, Kim SJ, Mehta H, Hevener AL, de Cabo R, Cohen P. Cell Metab. 2015;21(3):443–54. Model: in vitro (HEK293, HeLa, L6 myotubes) and rodent (C57BL/6 and CD-1 mice). PMID 25738459 · doi:10.1016/j.cmet.2015.02.009
18. Kim KH, Son JM, Benayoun BA, Lee C. The Mitochondrial-Encoded Peptide MOTS-c Translocates to the Nucleus to Regulate Nuclear Gene Expression in Response to Metabolic Stress. Cell Metab. 2018;28(3):516–524.e7. Model: in vitro. PMID 29983246 · doi:10.1016/j.cmet.2018.06.008
19. Reynolds JC, Lai RW, Woodhead JST, et al. Nat Commun. 2021;12(1):470. Model: rodent administration study (young, middle-aged and old mice), with human exercise measurements of endogenous expression. PMID 33473109 · doi:10.1038/s41467-020-20790-0
20. Elhusseiny R, Ihsan M, Labidi M, Alhammoud M, Mtibaa K, Nader N, Nasir N, Farooq A, Papakostas E, Olory B, Cruz F, D’Hooghe P, Racinais S, Deldicque L. Repeated Heat Stress Modulates the Levels of the Mitokines MOTS-C and FGF21 in Active Men during Calf Muscle Immobilization. Med Sci Sports Exerc. 2025;57(12):2764–74. Model: human randomised controlled trial; MOTS-c measured, not administered. PMID 40674654 · doi:10.1249/MSS.0000000000003825
21. Dieli-Conwright CM, et al. Effect of aerobic and resistance exercise on the mitochondrial peptide MOTS-c in Hispanic and Non-Hispanic White breast cancer survivors. Sci Rep. 2021;11(1):16916. Model: human randomised controlled trial; MOTS-c measured, not administered. PMID 34413391 · doi:10.1038/s41598-021-96419-z
22. von Walden F, et al. Acute endurance exercise stimulates circulating levels of mitochondrial-derived peptides in humans. J Appl Physiol (1985). 2021;131(3):1035–42. Model: human randomised controlled trial; MOTS-c measured, not administered. PMID 34351816 · doi:10.1152/japplphysiol.00706.2019
23. Cuyàs E, Verdura S, Martin-Castillo B, Menendez JA; METTEN study group. Circulating levels of MOTS-c in patients with breast cancer treated with metformin. Aging (Albany NY). 2022;15(4):892–7. Model: human randomised controlled trial; MOTS-c measured, not administered. PMID 36490309 · doi:10.18632/aging.204423
24. ClinicalTrials.gov, NCT07505745. A Phase 2a, Randomized, Double-blind, Placebo-controlled Study to Evaluate the Efficacy, Safety, and Pharmacodynamics of MOTS-c (a Mitochondrial-Derived Peptide) in Adults With Prediabetes and Overweight/Obesity. Sponsor: Hudson Biotech. Recruiting; estimated enrolment 120; start 2 February 2026; estimated primary completion February 2027. Model: trial registry record. clinicaltrials.gov
25. Covarrubias AJ, Perrone R, Grozio A, Verdin E. NAD+ metabolism and its roles in cellular processes during ageing. Nat Rev Mol Cell Biol. 2021;22(2):119–41. Model: review. PMID 33353981 · doi:10.1038/s41580-020-00313-x
26. Nikiforov A, Dölle C, Niere M, Ziegler M. Pathways and subcellular compartmentation of NAD biosynthesis in human cells: from entry of extracellular precursors to mitochondrial NAD generation. J Biol Chem. 2011;286(24):21767–78. Model: in vitro, human 293, HeLa S3 and HepG2 cells. PMID 21504897 · doi:10.1074/jbc.M110.213298
27. Martens CR, Denman BA, Mazzo MR, Armstrong ML, Reisdorph N, McQueen MB, Chonchol M, Seals DR. Nat Commun. 2018;9(1):1286. Model: human — randomised, double-blind, placebo-controlled crossover trial, n = 24. PMID 29599478 · doi:10.1038/s41467-018-03421-7
28. Elhassan YS, Kluckova K, Fletcher RS, et al. Cell Rep. 2019;28(7):1717–1728.e6. Model: human — randomised, double-blind, placebo-controlled crossover trial, n = 12. PMID 31412242 · doi:10.1016/j.celrep.2019.07.043
29. Brakedal B, Dölle C, Riemer F, et al. The NADPARK study: A randomized phase I trial of nicotinamide riboside supplementation in Parkinson’s disease. Cell Metab. 2022;34(3):396–407.e6. Model: human — double-blind randomised phase 1 trial, n = 30. PMID 35235774 · doi:10.1016/j.cmet.2022.02.001
30. Grant R, Berg J, Mestayer R, Braidy N, Bennett J, Broom S, Watson J. Front Aging Neurosci. 2019;11:257. Model: human — pilot study, n = 11 (8 receiving NAD+, 3 controls). PMID 31572171 · doi:10.3389/fnagi.2019.00257
31. Sun WD, Zhu XJ, Li JJ, Mei YZ, Li WS, Li JH. Nicotinamide N-methyltransferase (NNMT): a novel therapeutic target for metabolic syndrome. Front Pharmacol. 2024;15:1410479. Model: review. PMID 38919254 · doi:10.3389/fphar.2024.1410479
32. Neelakantan H, Vance V, Wetzel MD, Wang HL, McHardy SF, Finnerty CC, Hommel JD, Watowich SJ. Biochem Pharmacol. 2018;147:141–52. Model: in vitro and rodent (C57BL/6 mice). PMID 29155147 · doi:10.1016/j.bcp.2017.11.007
33. World Anti-Doping Agency. World Anti-Doping Code International Standard: Prohibited List 2026. Model: regulatory document. Sections S0 and S4.4.1 and the substance index were read directly. wada-ama.org
34. National Center for Biotechnology Information. PubChem Compound Summaries for CID 11764719 (elamipretide), CID 146675088 (MOTS-c), CID 5892 (NAD+) and CID 66522933 (5-amino-1-methylquinolinium iodide). Model: chemical database records. pubchem.ncbi.nlm.nih.gov