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5-Amino-1MQ

Also identified as 5-Amino-1-methylquinolinium, 5MQ

Small-molecule quinolinium cation

Published studies reviewed
4

FOR RESEARCH USE ONLY. NOT FOR HUMAN OR VETERINARY USE. NOT FOR HUMAN CONSUMPTION.

Compounds described on this site are supplied solely for laboratory research. They are not offered for human or veterinary use or for clinical use, and they are not intended to diagnose, mitigate, cure or prevent any disease.

5-Amino-1MQ is a small molecule rather than a peptide: a quinolinium cation methylated on its ring nitrogen and carrying an amino group at position 5, whose solid form is a salt with a counter-ion that has not been confirmed. This page reviews four preclinical publications, made up of enzyme selectivity and permeability assays, cultured-cell work and two mouse studies, all examining inhibition of nicotinamide N-methyltransferase. No human study of the molecule was found, so nothing recorded here describes an effect in a person.

At a glance

Also identified as
5-Amino-1-methylquinolinium, 5MQ
Class
Small-molecule quinolinium cation
Target or mechanism
Inhibitor — Nicotinamide N-methyltransferase (NNMT)
Evidence types represented
in vitro, animal
Published studies reviewed
4
Last reviewed
2026-09-21

Overview

5-Amino-1MQ is a small molecule, not a peptide: a quinolinium ring carrying a methyl group on its nitrogen and an amino group at position 5. It is a cation, so the solid material is a salt with a counter-ion.

⚠️ Its registry number, formula and mass are not recorded, because they differ between the cation and each salt, and which salt this material is has not been confirmed. None of the publications below states which salt it used.

Everything on this page is preclinical. The publications recorded here are enzyme assays, cultured-cell work and two studies in mice. No human study of this molecule was found, and none is recorded. A mouse figure does not become a human figure by being described carefully.

The molecule is studied as an inhibitor of one enzyme, nicotinamide N-methyltransferase (NNMT), which transfers a methyl group from S-adenosylmethionine to nicotinamide. That statement is backed by the enzyme and cell claims on this page, and by nothing else.

Mechanism under investigation

5-Amino-1MQ
Inhibitor
  • Nicotinamide N-methyltransferase (NNMT)

Recorded here as an inhibitor of nicotinamide N-methyltransferase. In cultured adipocytes it lowered the concentration of the enzyme's reaction product 1-methylnicotinamide and raised intracellular NAD+ and S-adenosylmethionine, and in a panel of related enzymes it did not inhibit DNMT1, PRMT3, NAMPT or SIRT1. The publications recorded here do not describe a receptor, and no human data exist for any of this.

Scope of the published work

Areas investigated
  • Enzyme inhibition and selectivity
  • Membrane permeability
  • Adipocyte metabolite concentrations
  • Body weight and adipose tissue mass in mice
  • Skeletal muscle in aged mice
  • Cell proliferation in a cancer cell line
Models used
  • Recombinant enzyme assays
  • 3T3-L1 pre-adipocytes and adipocytes
  • Caco-2 and artificial membrane permeability assays
  • Diet-induced obese mice
  • Aged mice
  • HeLa and HEK-293 cell lines

Every figure on this page was measured in an enzyme assay, a cell culture or a mouse. No human study of this molecule is recorded here, and nothing on this page establishes anything about a person. It is not a statement about the research material PepGenex supplies.

Limitations

Evidence represented on this page: in vitro and animal. No human research is represented. The page reviews 4 published studies, and each figure is reported for the study that published it; results are not pooled across studies. 1 of these publications carries a note on whether it studied this exact material.

Common questions

What is 5-Amino-1MQ?

5-Amino-1MQ is a small molecule, not a peptide: a quinolinium ring carrying a methyl group on its nitrogen and an amino group at position 5.

How does 5-Amino-1MQ work, according to the published research?

Recorded here as an inhibitor of nicotinamide N-methyltransferase. In cultured adipocytes it lowered the concentration of the enzyme's reaction product 1-methylnicotinamide and raised intracellular NAD+ and S-adenosylmethionine, and in a panel of related enzymes it did not inhibit DNMT1, PRMT3, NAMPT or SIRT1. The publications recorded here do not describe a receptor, and no human data exist for any of this.

  • A screen of N-methylated quinolinium, isoquinolinium, pyridinium and benzimidazolium / benzothiazolium analogues identified the quinoliniums as a scaffold reaching very low micromolar inhibition of nicotinamide N-methyltransferase (IC50 about 1 µM), across a series whose activity spanned more than a thousandfold. Computer-based docking to the enzyme's nicotinamide-binding site correlated with the measured IC50 values, and the predicted binding orientation placed the quinolinium analogues at that substrate-binding site. (Neelakantan et al., 2017, PMID 28548833)

What has published research on 5-Amino-1MQ found, and what are its limits?

This page records 4 publications, reporting laboratory (in vitro) work in 3, animal work in 2. Each is listed with its identifier under References.

No human study is represented on this page.

Evidence represented on this page: in vitro and animal.

No human research is represented.

The page reviews 4 published studies, and each figure is reported for the study that published it; results are not pooled across studies.

1 of these publications carries a note on whether it studied this exact material.

Every figure on this page was measured in an enzyme assay, a cell culture or a mouse. No human study of this molecule is recorded here, and nothing on this page establishes anything about a person. It is not a statement about the research material PepGenex supplies.

Is 5-Amino-1MQ approved by the U.S. FDA?

This page cites no FDA approval record for 5-Amino-1MQ; PepGenex Science states a U.S. regulatory status only where a sourced record exists.

PepGenex research materials are not FDA approved and are not for human or veterinary use.

What risks have published studies of 5-Amino-1MQ reported?

No human study is recorded on this page, so it reports no adverse events in people. Laboratory and animal findings are not a measure of risk in people.

Published research

Grouped by the kind of study. Select one to narrow what is shown below.

Laboratory (in vitro)(2)

Laboratory (in vitro)

Small molecule inhibitor of nicotinamide N-methyltransferase shows anti-proliferative activity in HeLa cells.

Akar S, Duran T, Azzawri AA, Koçak N, Çelik Ç, Yıldırım Hİ., Journal of Obstetrics and Gynaecology, 2021;41(8):1240-1245

published

5-amino-1-methylquinolinium was tested at 0.1 to 500 µM on the HeLa epithelial cervical cancer cell line, with viability assessed by MTT assay and mRNA and protein levels of TWIST, ZEB1, SERPIN1, SIRT1 and CD16 measured by quantitative real-time PCR and Western blotting.

  • Proliferation of HeLa cells was inhibited significantly, in a manner dependent on concentration and time, while proliferation of HEK-293 cells was not apparently affected. Cells showed increased shrinkage, loss of cellular adhesions and apoptotic bodies. ZEB1, SIRT1 and CD16 mRNA levels rose while TWIST and SERPIN1 mRNA levels fell, and the phospho-Akt and SIRT1 proteins decreased. The abstract reports no IC50 and no per-concentration values.
Limitations

Three of the four publications come from one group at the University of Texas Medical Branch, and the authors of the later papers disclose a commercial interest in developing inhibitors of this enzyme. The fourth, from an independent group, is a cell-line study that reports direction and significance without printing a number. Independent replication of the animal findings is what this page does not have.

View publication →
Laboratory (in vitro)

Structure-Activity Relationship for Small Molecule Inhibitors of Nicotinamide N-Methyltransferase.

Neelakantan H, Wang HY, Vance V, Hommel JD, McHardy SF, Watowich SJ., Journal of Medicinal Chemistry, 2017;60(12):5015-5028

published

Material identity not established. This paper's abstract describes a screen of methylated quinolinium and related analogues and does not name 5-amino-1MQ individually. The compound is one of that series: the 2018 paper on this page names 5-amino-1MQ, cites this paper for its IC50 of about 1 µM, and shares five of its six authors. The claim recorded from this source is therefore about the series, not about this molecule alone.

  • A screen of N-methylated quinolinium, isoquinolinium, pyridinium and benzimidazolium / benzothiazolium analogues identified the quinoliniums as a scaffold reaching very low micromolar inhibition of nicotinamide N-methyltransferase (IC50 about 1 µM), across a series whose activity spanned more than a thousandfold. Computer-based docking to the enzyme's nicotinamide-binding site correlated with the measured IC50 values, and the predicted binding orientation placed the quinolinium analogues at that substrate-binding site.
View publication →

Preclinical (animal)(2)

Preclinical (animal)

Small molecule nicotinamide N-methyltransferase inhibitor activates senescent muscle stem cells and improves regenerative capacity of aged skeletal muscle.

Neelakantan H, Brightwell CR, Graber TG, Maroto R, Wang HL, McHardy SF, Papaconstantinou J, Fry CS, Watowich SJ., Biochemical Pharmacology, 2019;163:481-492

published

24-month-old mice received saline, or 5-amino-1MQ (two groups), for 1 week after an induced injury to the tibialis anterior muscle, or saline or 5-amino-1MQ for 3 weeks after injury. All mice received 5-ethynyl-2'-deoxyuridine systemically so that muscle stem cell activity could be tracked. Contractile function was measured in vivo in the injured muscle and myofiber cross-sectional area ex vivo.

  • Muscle stem cell proliferation and subsequent fusion were higher in the mice given the inhibitor, with nearly 2-fold greater myofiber cross-sectional area and a shift in fiber size distribution toward larger fibers compared with controls; the longer 3-week schedule produced larger cross-sectional area still. Peak torque of the tibialis anterior was about 70 % greater than in controls. Comparable changes were seen in cultured C2C12 myoblasts, alongside changes in the cellular NAD+/NADH redox state.
Limitations

There is no human study of this molecule on this page because this project found none. The mouse figures were measured in 11 days in obese mice and in aged mice after a muscle injury, in groups housed and fed under laboratory control, and they are reported here as what they are: animal results. Nothing establishes that any of it happens in a person.

View publication →
Laboratory (in vitro)Preclinical (animal)

Selective and membrane-permeable small molecule inhibitors of nicotinamide N-methyltransferase reverse high fat diet-induced obesity in mice.

Neelakantan H, Vance V, Wetzel MD, Wang HL, McHardy SF, Finnerty CC, Hommel JD, Watowich SJ., Biochemical Pharmacology, 2018;147:141-152

published

An 11-day proof-of-concept study in male diet-induced obese mice, 17 weeks old and fed a high-fat diet from week 6. Mice received either saline or 5-amino-1MQ for 11 days; food intake and body weight were recorded, and epididymal white adipose tissue and plasma lipids were measured at the end.

Cumulative change in body weight
Preclinical · Day 11 · Male diet-induced obese C57BL/6 mice, fed a high-fat diet from week 6 and 17 weeks old at study start
ArmReported
saline control+0.6 ± 0.4 g (about 1.4 % of baseline)
5-amino-1MQ-2.0 ± 0.6 g (about 5.1 % of baseline)
  • In parallel artificial membrane and Caco-2 cell assays, 5-amino-1MQ showed high passive and active transport across membranes with no detectable efflux, while the unsubstituted parent analogue 1-methylquinolinium and the enzyme's reaction product 1-methylnicotinamide showed no passive permeability.
  • Against a panel of structurally related methyltransferases and two enzymes of the NAD+ salvage pathway, 5-amino-1MQ did not inhibit DNMT1 or PRMT3 at concentrations from 10 nM to 600 µM, did not inhibit NAMPT up to 100 µM, and did not inhibit SIRT1 from 10 nM to 300 µM, with a minor reduction in SIRT1 activity at 600 µM. Inhibition of COMT reached 10 % at the maximum tested concentration of 600 µM. No IC50 could be fitted for any of them, because no significant inhibition was observed.
  • In fully differentiated 3T3-L1 adipocytes, 5-amino-1MQ lowered the intracellular concentration of the enzyme's reaction product 1-methylnicotinamide in a concentration-dependent way, with a fitted EC50 of 2.3 ± 1.1 µM. Over 1 to 60 µM it raised intracellular NAD+ by about 1.2 to 1.6-fold relative to control adipocytes, and at 30 µM and 60 µM it reduced lipid accumulation in differentiating pre-adipocytes by 50 % and 70 % respectively (P = 0.0001). Cell viability was only slightly reduced at the highest concentration tested (P < 0.05).
  • Body weight differed significantly between the groups on days 6 (P < 0.01), 9 (P < 0.0001) and 10 (P < 0.0001). Food intake did not differ (28.1 ± 1.2 g cumulative in controls against 26.2 ± 1.4 g; P > 0.05). Epididymal white adipose tissue mass was about 35 % lower in the 5-amino-1MQ group (P < 0.001), adipocyte size was more than 30 % smaller (P < 0.05), and plasma total cholesterol was about 30 % lower (P < 0.05).
Limitations

There is no human study of this molecule on this page because this project found none. The mouse figures were measured in 11 days in obese mice and in aged mice after a muscle injury, in groups housed and fed under laboratory control, and they are reported here as what they are: animal results. Nothing establishes that any of it happens in a person.

Context

The selectivity panel is a set of negative results, and that is its value: across DNMT1, PRMT3, NAMPT and SIRT1 no inhibition could be fitted at all. It says what the molecule did not do to four related enzymes in an assay. It does not establish what it does in a living animal, let alone a person.

View publication →

Compared with related compounds

Classification, structure, recorded targets, evidence types and FDA status only, each read from the two compounds' own pages. These comparisons do not compare study results.

5-Amino-1MQ and NAD+

Related through one enzyme: 5-amino-1MQ is recorded as an inhibitor of nicotinamide N-methyltransferase; NAD+ is the coenzyme its studies measured.

5-Amino-1MQNAD+
ClassificationSmall-molecule quinolinium cationDinucleotide coenzyme
StructureNot recorded on its pageFormula C21H27N7O14P2
Targets recordedInhibitor: Nicotinamide N-methyltransferase (NNMT)No target recorded on its page
Evidence types representedin vitro, animalin vitro, human
Status with the U.S. FDANot shown (no Drugs@FDA application record verified for this page)Not shown (no Drugs@FDA application record verified for this page)

References

Published studies reviewed (4)

  1. Structure-Activity Relationship for Small Molecule Inhibitors of Nicotinamide N-Methyltransferase. — Neelakantan H, Wang HY, Vance V, Hommel JD, McHardy SF, Watowich SJ., Journal of Medicinal Chemistry, 2017;60(12):5015-5028
    DOI 10.1021/acs.jmedchem.7b00389 · PMID 28548833
  2. Selective and membrane-permeable small molecule inhibitors of nicotinamide N-methyltransferase reverse high fat diet-induced obesity in mice. — Neelakantan H, Vance V, Wetzel MD, Wang HL, McHardy SF, Finnerty CC, Hommel JD, Watowich SJ., Biochemical Pharmacology, 2018;147:141-152
    DOI 10.1016/j.bcp.2017.11.007 · PMID 29155147 · PMC5826726
  3. Small molecule nicotinamide N-methyltransferase inhibitor activates senescent muscle stem cells and improves regenerative capacity of aged skeletal muscle. — Neelakantan H, Brightwell CR, Graber TG, Maroto R, Wang HL, McHardy SF, Papaconstantinou J, Fry CS, Watowich SJ., Biochemical Pharmacology, 2019;163:481-492
    DOI 10.1016/j.bcp.2019.02.008 · PMID 30753815 · PMC6469996
  4. Small molecule inhibitor of nicotinamide N-methyltransferase shows anti-proliferative activity in HeLa cells. — Akar S, Duran T, Azzawri AA, Koçak N, Çelik Ç, Yıldırım Hİ., Journal of Obstetrics and Gynaecology, 2021;41(8):1240-1245
    DOI 10.1080/01443615.2020.1854696 · PMID 33645410

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