All information below describes the compound's chemical identity, laboratory handling, and the published research literature. It describes molecular targets and results in laboratory and animal models only — not effects in humans — and is not evidence of any human benefit.
What Is 5-Amino-1MQ?
5-Amino-1MQ (5-amino-1-methylquinolinium) is a non-peptide small-molecule compound, supplied as the iodide salt (molecular formula C10H10IN2; MW 286.09 g/mol; CAS 1048980-98-8). As a small molecule rather than a peptide, it has no amino-acid sequence. It is characterized in the published literature as a competitive inhibitor of nicotinamide N-methyltransferase (NNMT), an enzyme associated with cellular methylation and one-carbon metabolic pathways.
It is supplied as a reference compound for in vitro and animal research use only. The sections below summarize its chemical identity, laboratory handling, the molecular targets and model systems examined in the published literature, and the primary references — without describing outcomes, efficacy, or effects in humans.
Research Targets & Pathways
Published preclinical literature has examined 5-Amino-1MQ in relation to several molecular systems. These are pathway associations reported in laboratory and animal models; refer to the cited studies for methods and findings.
- Nicotinamide N-methyltransferase (NNMT) — examined as a competitive enzyme-inhibition target within cellular methylation and one-carbon metabolism.
- NAD+ cofactor pool — examined in relation to intracellular nicotinamide adenine dinucleotide availability.
- S-adenosylmethionine (SAM) / methyl-donor pool — examined in relation to methyl-group consumption and methylation capacity.
- SIRT1 signaling — examined in relation to sirtuin pathway activity in NNMT-knockdown model systems.
- TGF-β signaling — examined in relation to fibrotic pathway activity in renal tubular-cell systems.
- Glucocorticoid signaling — examined in relation to the early phase of adipocyte differentiation in cell culture.
- Senescence markers (p21/p16, SASP) — examined in relation to senescence-associated signaling in stromal-cell systems.
Model Systems Studied
5-Amino-1MQ and related NNMT inhibitors have been used as test compounds across a range of published preclinical model systems, primarily in rodents, invertebrate models, and in vitro cell assays. Refer to the cited literature for study designs, endpoints, and findings.
- Invertebrate — C. elegans NNMT-knockdown model systems.
- Rodent metabolic — high-fat-diet mouse obesity models and white-adipose-tissue knockdown models.
- In vitro adipogenesis — 3T3-L1 preadipocyte differentiation and lipid-droplet assay systems.
- Renal — renal tubular-cell fibrosis systems and early-stage chronic-kidney-disease models.
- Senescence cell culture — stromal-cell systems profiling senescence-associated markers.
- Oncology — breast-cancer cell lines and tumor model systems.
- Tissue metabolic profiling — hepatic and adipose tissue in metabolic-disease models.
Note: several of the more recent NNMT-inhibitor citations are from 2026 preprint or early-access publications, and independent replication status should be verified; some senescence findings are derived from stromal-cell culture systems and have not been validated in clinical populations.
Molecular & Technical Profile
C10H10IN2 (iodide salt) | MW 286.09 g/mol | CAS 1048980-98-8 | Non-peptide small molecule (no amino-acid sequence)
Storage, Reconstitution & Working Concentrations
Storage, reconstitution, and working-concentration values are general laboratory guidance for in vitro and animal research; always confirm against the lot-specific Certificate of Analysis.
Current Research Status
As of the time of this writing, 5-Amino-1MQ has not been approved by the U.S. Food and Drug Administration (FDA) for any human therapeutic use, and published reviews note that no NNMT-targeting compound has received regulatory approval for human use; all findings to date remain preclinical, derived from in vitro assays and animal models. The research-grade material supplied by Explicit Research is a reference compound for laboratory research use only and is not an approved drug product. Several of the more recent NNMT-inhibitor citations are from 2026 preprint or early-access publications, and independent replication status should be verified before citation in downstream research.
Research FAQ
Is 5-Amino-1MQ approved for human use?
No. 5-Amino-1MQ has not been approved by the FDA for any human therapeutic use, and published reviews note that no NNMT-targeting compound has received regulatory approval for human use. The evidence base is preclinical (in vitro and animal models), and the compound is supplied for laboratory research use only — not for human consumption.
What is 5-Amino-1MQ's molecular formula and sequence?
A non-peptide small molecule with no amino-acid sequence, supplied as the iodide salt — molecular formula C10H10IN2, MW 286.09 g/mol, CAS 1048980-98-8.
How is 5-Amino-1MQ stored and reconstituted?
Store the sealed solid at room temperature (15–25°C) or 2–8°C, protected from light and moisture. As a small molecule it is dissolved in DMSO to a stock concentration, then diluted stepwise into aqueous buffer or culture medium; keep the final DMSO concentration at or below 0.1% v/v and avoid repeated freeze–thaw.
What targets and model systems has 5-Amino-1MQ been studied in?
Preclinical work has characterized 5-Amino-1MQ as a competitive NNMT (nicotinamide N-methyltransferase) inhibitor, examined in relation to NAD+ and methyl-donor (SAM) pools across C. elegans, rodent metabolic, 3T3-L1 adipogenesis, renal fibrosis, senescence cell-culture, and oncology model systems. Note the 2026 preprint/early-access replication caveat noted above.
Selected References
- Aksoy et al. — Crystal structure of human nicotinamide N-methyltransferase with bound substrates characterizing the active site. Biochemistry, 2004.
- Aksoy et al. — Identification and characterization of NNMT enzyme kinetics and substrate binding interactions. Drug Metab Dispos, 2006.
- Ulanovskaya et al. — NNMT activity and methylation capacity measured in cancer cell lines using chemical proteomics approaches. Nat Chem Biol, 2013.
- Neelakantan et al. — Small molecule inhibitor of NNMT with cellular target engagement measured in adipocytes. ACS Med Chem Lett, 2017.
- Schmeisser et al. — NNMT knockdown in C. elegans measured effects on NAD+ levels, lifespan extension, and SIRT1 pathway activation. Aging, 2013.
- Eckert et al. — NNMT activity and methyl group consumption measured in hepatic and adipose tissue in metabolic disease models. J Proteome Res, 2012.
- Kannt et al. — NNMT expression measured in adipose tissue of obese humans; association with reduced NAD+ and SAM availability assessed. Diabetes Metab Res Rev, 2015.
- Kraus et al. — NNMT inhibitors reverse high fat diet-induced obesity in mice, measuring cellular NAD+ levels and suppression of fat production. Biochem Pharmacol, 2018.
- Halperin et al. — NNMT silencing in white adipose tissue measured resting metabolic rate, lipid mobilization, and body weight in mouse models. Nature, 2013.
- Park et al. — NNMT regulation of the glucocorticoid signaling pathway measured during the early phase of adipogenesis in cell culture. Sci Rep, 2023.
- Campagna et al. — NNMT expression and TGF-beta pathway activation measured in renal tubular cells under fibrotic conditions. J Am Soc Nephrol, 2019.
- Roberti et al. — Senescence-associated secretory phenotype (SASP) markers and p21/p16 expression quantified after NNMT modulation in stromal cells. Aging Cell, 2020.
- Zhang et al. — NNMT expression, proliferation markers, and pathway signaling measured in breast cancer cell lines and tumor models. Biochem Pharmacol, 2026.
- Li et al. — NNMT as a therapeutic target in fibrosis; collagen deposition and fibrotic pathway activity measured across cardiac, hepatic, renal, and pulmonary models. Differentiation, 2026.
- Vaquero-Vara et al. — NNMT inhibition measured against tubular senescence markers and fibrotic gene expression in early-stage chronic kidney disease models. Cell Rep, 2026.
- Wen et al. — Structure-based drug discovery of non-SAM-mimetic bisubstrate inhibitors against nicotinamide N-methyltransferase. ACS Med Chem Lett, 2026.
- Teng et al. — Emerging opportunities for nicotinamide N-methyltransferase (NNMT) inhibitor clinical translation; review noting that no NNMT-targeting compound has received regulatory approval for human use. Trends Pharmacol Sci, 2026.
