A small-molecule inhibitor of nicotinamide N-methyltransferase, an enzyme that disposes of nicotinamide and therefore sits upstream of NAD+ availability.
- Compound
- 5-amino-1-methylquinolinium, a small-molecule NNMT inhibitor (not a peptide)
- Molecular formula
- C10H11N2+ (cation); supplied as a salt, with the counter-ion stated on the batch Certificate of Analysis
- Molecular weight
- 159.2 g/mol (cation)
- Appearance
- lyophilised powder
- Strengths available
- 5mg, 10mg per vial
- Released against
- the Certificate of Analysis for its own batch
Purity is established by HPLC and identity by mass spectrometry, as for the rest of the catalogue.
About 5-Amino-1MQ
5-Amino-1-methylquinolinium is not a peptide, which is worth stating plainly because it sits in a peptide catalogue and is often described as one. It is a small quaternary quinolinium compound with a permanent positive charge on the ring nitrogen, so it is prepared as a salt.
Its target is nicotinamide N-methyltransferase (NNMT), which methylates nicotinamide to 1-methylnicotinamide and removes it from the salvage pathway that regenerates NAD+. An enzyme that disposes of the main NAD+ precursor is, in effect, a drain on NAD+ supply, so inhibiting it is predicted to raise intracellular nicotinamide and, downstream, NAD+. NNMT is highly expressed in adipose tissue and liver, and its expression rises in obesity models and several cancers, which is what made it a target.
What the research covers
Work covers NNMT enzyme kinetics and inhibitor selectivity, intracellular NAD+ and 1-methylnicotinamide as the direct readouts, and downstream adipocyte endpoints including lipolysis, differentiation and adipocyte size, with sirtuin activity as a secondary readout. Because it acts on an enzyme rather than a receptor, the informative measurement is the metabolite ratio, and work reporting only downstream phenotype is hard to interpret.
It addresses the same metabolic axis as NAD+ from the other direction: NAD+ supplies the cofactor, 5-Amino-1MQ stops the cell wasting its precursor, so running both can distinguish supply-limited from disposal-limited conditions. Published work is preclinical and largely in rodents; there is no clinical trial literature, and quantitative claims circulating about it outrun the evidence. A separate oncology literature on NNMT is mechanistically relevant and often overlooked. Published work is indexed on PubMed.
Handling 5-Amino-1MQ
As a small molecule this is considerably more robust than the peptides stored alongside it and does not share their adsorption behaviour at low working concentration. Keep it dry and sealed.
Solubility rather than stability is the practical constraint: quinolinium salts dissolve readily in aqueous buffer, but the useful concentration range should be established before a protocol depends on it. Solvent options are under reconstitution supplies.
Common questions about 5-Amino-1MQ
Is 5-Amino-1MQ a peptide?
No. It is a small quinolinium compound that inhibits an enzyme. It is listed with the metabolic peptides because of the research questions it addresses.
What does NNMT do?
Nicotinamide N-methyltransferase methylates nicotinamide, removing it from the pathway that recycles it into NAD+.
How does it relate to NAD+?
Blocking NNMT keeps more nicotinamide available for NAD+ synthesis. It approaches NAD+ availability by reducing disposal rather than adding supply.
What should be measured in 5-Amino-1MQ studies?
The direct readouts: intracellular NAD+ and 1-methylnicotinamide. Downstream phenotype without those is hard to interpret.
How should it be stored?
Dry and sealed. As a small molecule it is more robust than the peptides in the catalogue.
