5-Amino-1MQ Research, Specifications & Scientific Information

Introduction

5-Amino-1MQ is a 159-dalton charged ring system that inhibits one enzyme, and the interest in it comes from what that enzyme sits between.

Nicotinamide N-methyltransferase transfers a methyl group from S-adenosylmethionine onto nicotinamide. That single reaction consumes two things a cell values: the universal methyl donor, and the nicotinamide that would otherwise be recycled into NAD+. Blocking the enzyme should therefore raise both — and in cultured adipocytes it does, along with reducing the reaction's product, 1-methylnicotinamide ^[1].

The compound has no human literature. None has been identified in public trial registers or in the peer-reviewed record. Everything on this page is cell culture and mice, tiered accordingly, and the page is short because the evidence is.

It describes research. It contains no guidance of any kind on handling the material.

What Is 5-Amino-1MQ?

A small synthetic molecule: 5-amino-1-methylquinolin-1-ium. Not a peptide, and listed in this library under peptide-adjacent research compounds.

Structurally it is a quinoline whose ring nitrogen has been methylated, which leaves that nitrogen permanently positively charged, with a primary amine at position 5. Both features are load-bearing:

The permanent charge is the pharmacophore. A quaternised nitrogen on an aromatic ring is a reasonable mimic of 1-methylnicotinamide, the methylated product the target enzyme releases. Product-like inhibitors of methyltransferases are a standard design, and this is one.

The amine is what gets it into cells. Permanently charged molecules usually cross membranes poorly. The discovery work reported that methylquinolinium scaffolds with primary amine substitutions showed high permeability in both passive and active transport assays, which is what made the series viable at all ^[1].

Because the cation cannot exist alone, the compound is always supplied as a salt — most often the iodide, which the register separately names NNMTi. It is not an approved medicine anywhere and has never been in a clinical trial.

5-Amino-1MQ Specifications

5-Amino-1MQ is a small quaternary heteroaromatic cation, not a peptide. The FDA/NCATS Global Substance Registration System carries the cation under UNII PMX593N4N3 with CAS registry number 685079-15-6 and PubChem compound identifier 950107, molecular formula C10H11N2 as a cation and a mass of 159.21 g/mol. Because the molecule carries a permanent positive charge on its quaternised ring nitrogen, it cannot exist on its own and is always supplied as a salt. Two salt records exist in the same register: the iodide, UNII K9G33W2TTZ, CAS registry number 42464-96-0, PubChem compound identifier 66522933, formula C10H11N2·I and mass 286.11 g/mol — which is also the form the register names NNMTi — and a chloride, UNII KK7LU6YQL5. The iodide is roughly 80 per cent heavier than the cation, so a quantity stated without naming the salt is ambiguous by that margin. The permanent charge is not incidental to the pharmacology: it is what makes the molecule a mimic of the methylated reaction product of the enzyme it inhibits, and the primary amine at position 5 is what the discovery work identified as conferring membrane permeability on an otherwise charged scaffold.

Values that a public register does not carry are shown as not publicly characterised rather than estimated. Identifiers are reference values; the certificate of analysis supplied with a laboratory order is the record for a given lot.

How Does 5-Amino-1MQ Work?

By inhibiting nicotinamide N-methyltransferase, a cytosolic enzyme that is abundant in liver and in adipose tissue.

The reaction it catalyses is simple and its position in metabolism is what makes it interesting. Nicotinamide plus S-adenosylmethionine gives 1-methylnicotinamide plus S-adenosylhomocysteine. Nicotinamide is the substrate of the NAD+ salvage pathway, so methylating it removes it from that pathway; S-adenosylmethionine is the methyl donor for essentially every methylation in the cell, so consuming it draws on a shared pool.

Inhibiting the enzyme should therefore push both quantities up, and the published cell work reports exactly that: reduced intracellular 1-methylnicotinamide alongside increased intracellular NAD+ and S-adenosylmethionine ^[1].

Two cautions belong here. The proposed downstream account — that increased flux of NAD+ and S-adenosylmethionine explains the metabolic effects — was offered by the original authors as a possibility rather than a demonstration, and their own wording is conditional. And the readout that most directly confirms target engagement is the fall in 1-methylnicotinamide, not the rise in NAD+, because the fall is the enzyme's own product and the rise has other possible causes.

5-Amino-1MQ Mechanism of Action

In vitro research

The characterisation study examined a series of small-molecule inhibitors of the enzyme across four dimensions, and the design is worth setting out because each dimension answers a specific objection.

Permeability. Assessed by parallel artificial membrane permeability assay and by Caco-2 cell assay — a passive measure and an active-transport measure. Methylquinolinium scaffolds with primary amine substitutions showed high permeability in both ^[1].

Selectivity. Tested against structurally related methyltransferases and against enzymes of the NAD+ salvage pathway. The analogues inhibited neither ^[1]. Those two families are the obvious places for a nicotinamide-like inhibitor to go wrong, so testing them is the right control — though it is a targeted check rather than a broad selectivity panel.

Target engagement in cells. In cultured adipocytes, the inhibitors reduced intracellular 1-methylnicotinamide and raised intracellular NAD+ and S-adenosylmethionine ^[1].

Cellular consequence. Lipogenesis in cultured adipocytes was suppressed ^[1].

Separate work has reported anti-proliferative activity for a nicotinamide N-methyltransferase inhibitor in HeLa cells ^[2], and the medicinal chemistry of this inhibitor class has been reviewed ^[3].

What Is 5-Amino-1MQ Being Researched For?

Two lines, both preclinical.

• Adipose tissue and metabolic phenotype in diet-induced obese mice. The main line, including a combination study with a diet substitution and an associated microbiome analysis ^{[1, 4, 5]}.
• The enzyme as a target, more broadly. Reviews and further inhibitor work place nicotinamide N-methyltransferase in metabolic syndrome and in oncology contexts ^{[3, 6, 7, 2]}.

There is no human research on this compound. No clinical trial, no registered study, no published human pharmacokinetics. That absence is the most important single fact on this page, and this page does not fill it with findings about the enzyme obtained by other means.

A further point of context: much of the mouse work comes from one academic group at the University of Texas Medical Branch and from a company founded by its senior author, with those interests declared in the papers themselves. A concentrated authorship is not a criticism of any individual result; it is a reason that independent replication carries more weight than an additional study from the same source.

Preclinical Research on 5-Amino-1MQ

Animal research

The validation study. A potent inhibitor of this series was administered systemically to diet-induced obese mice fed a high-fat diet. Reported outcomes were significantly reduced body weight and white adipose mass, decreased adipocyte size, and lowered plasma total cholesterol. Two negative observations were reported alongside: administration did not affect total food intake, and no observable adverse effects were produced ^[1].

Why the food intake result matters. An intervention that reduces body mass in mice by making them eat less is a different kind of finding from one that does so without changing intake. Reporting intake explicitly is what allows a reader to distinguish the two, and its absence in a study of this kind would be a gap.

Combination with a diet substitution. Inhibitor treatment combined with substituting a lean diet in diet-induced obese mice accelerated and improved body weight and fat loss, increased the whole-body lean mass to body weight ratio, reduced liver and epididymal white adipose tissue weights, decreased liver adiposity and improved hepatic steatosis, relative to the diet substitution alone. The combination normalised body composition and liver adiposity to the values seen in age-matched lean-diet control mice. Adipose tissue showed a distinct metabolomic signature, with increases in ketogenic amino acid abundance ^[4].

The microbiome analysis. The same combination established a distinct gut microbiome in diet-induced obese mice ^[5], which is reported here as an observed correlate rather than as a mechanism.

Beyond adipose tissue. Inhibition of the enzyme has been examined more broadly in obesity-related metabolic dysfunction ^[7].

Findings described in this section were observed in animals, and nothing in them establishes anything about humans. Diet-induced obesity in mice is a standard preclinical model and a historically poor predictor of human results in metabolic pharmacology.

Current Research Status

Status as of September 22, 2026. This block is rendered from maintained fields, not from prose, so it cannot go stale in one place and stay current in another.

5-Amino-1MQ vs Related Compounds

The comparisons below are structural, mechanistic and evidential. No comparison of effect is made on this page.

NAD+ and its precursors :: Approach the same cofactor pool from the opposite direction — supplying substrate rather than blocking its removal. NAD+ precursors have reached randomised controlled trials in humans; this compound has reached none. AICAR :: Also a small molecule acting on cellular metabolic regulation, and also not a peptide. AICAR has a completed phase 3 trial with a null result; this compound has no human data at all. Both illustrate how far the evidence positions within one category can diverge. SLU-PP-332 :: The closest match in this library for evidence position — a synthetic small molecule with an identified molecular target, a mouse literature, and no human studies.

Chemical class

A 159-dalton quaternary quinolinium cation. It appears in a peptide library because of the research questions it is used to ask, not because of any structural relationship to the peptides here.

Chemical & Molecular Characteristics

Three register records, one compound. The cation is UNII PMX593N4N3, CAS registry number 685079-15-6, PubChem compound identifier 950107, formula C10H11N2⁺, 159.21 g/mol. The iodide salt is UNII K9G33W2TTZ, CAS registry number 42464-96-0, PubChem compound identifier 66522933, formula C10H11N2·I, 286.11 g/mol — and it is under that record that the register carries the name NNMTi. A chloride salt is registered separately under UNII KK7LU6YQL5.

The salt difference is large. Iodide is a heavy counter-ion: the salt is roughly 80 per cent heavier than the cation it carries. A figure quoted for this compound without specifying the form is ambiguous by that margin, which is a greater discrepancy than for most salt pairs in this library.

The charge is permanent, not pH-dependent. A quaternised ring nitrogen has no lone pair to protonate or deprotonate. That distinguishes this molecule from ordinary amines, whose charge state varies with pH, and it is the structural reason the compound resembles the enzyme's methylated product.

The sequence fields are blank because there is no sequence. This is a synthetic heteroaromatic small molecule with no amino acids in it.

Frequently Asked Questions

Scientific References

1. Neelakantan H, Vance V, Wetzel MD, et al.. Selective and membrane-permeable small molecule inhibitors of nicotinamide N-methyltransferase reverse high fat diet-induced obesity in mice Biochemical pharmacology; 2018. PMID 29155147 doi:10.1016/j.bcp.2017.11.007
2. Akar S, Duran T, Azzawri AA, et al.. Small molecule inhibitor of nicotinamide N-methyltransferase shows anti-proliferative activity in HeLa cells Journal of obstetrics and gynaecology : the journal of the Institute of Obstetrics and Gynaecology; 2021. PMID 33645410 doi:10.1080/01443615.2020.1854696
3. Kannt A, Rajagopal S, Hallur MS, et al.. Novel Inhibitors of Nicotinamide-N-Methyltransferase for the Treatment of Metabolic Disorders Molecules (Basel, Switzerland); 2021. PMID 33668468 doi:10.3390/molecules26040991
4. Sampson CM, Dimet AL, Neelakantan H, et al.. Combined nicotinamide N-methyltransferase inhibition and reduced-calorie diet normalizes body composition and enhances metabolic benefits in obese mice Scientific reports; 2021. PMID 33707534 doi:10.1038/s41598-021-85051-6
5. Dimet-Wiley A, Wu Q, Wiley JT, et al.. Reduced calorie diet combined with NNMT inhibition establishes a distinct microbiome in DIO mice Scientific reports; 2022. PMID 35013352 doi:10.1038/s41598-021-03670-5
6. Sun WD, Zhu XJ, Li JJ, et al.. Nicotinamide N-methyltransferase (NNMT): a novel therapeutic target for metabolic syndrome Frontiers in pharmacology; 2024. PMID 38919254 doi:10.3389/fphar.2024.1410479
7. Babula JJ, Bui D, Stevenson HL, et al.. Nicotinamide N-methyltransferase inhibition mitigates obesity-related metabolic dysfunction Diabetes, obesity & metabolism; 2024. PMID 39161060 doi:10.1111/dom.15879

Every identifier above is resolved against PubMed, Crossref or ClinicalTrials.gov at build time, and the title returned by the register is compared with the title stored here. A page does not publish if a reference fails to resolve.

Research-Use Information

For in vitro research use only. This material is a laboratory reagent. It is not a drug, food, dietary supplement, or cosmetic and is not for human or veterinary use, including ingestion, injection, or any other administration. No information on this page describes or implies any effect in humans or animals. Sold only to researchers under our Terms of Sale.