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5-AMINO-1MQ - 50mg
Overview
5-Amino-1MQ (5-amino-1-methylquinolinium) is a synthetic, cell-permeable small molecule investigated as a selective inhibitor of nicotinamide N-methyltransferase (NNMT), an enzyme involved in the methylation of nicotinamide and regulation of NAD+ availability. It is classified as a research compound and is not FDA-approved. Current evidence is primarily derived from preclinical cell-based and animal studies.
Mechanism of Action
By inhibiting NNMT, 5-Amino-1MQ preserves intracellular NAD+ levels by preventing the conversion of nicotinamide to 1-methylnicotinamide (1-MNA). Elevated NAD+ availability activates SIRT1 (sirtuin-1) pathways associated with mitochondrial biogenesis, fat oxidation, and metabolic flexibility. Simultaneously, higher S-adenosylmethionine (SAM) availability supports methylation-dependent gene expression and epigenetic regulation.
Research and Off-Label Applications
Investigated for reduction of visceral and white adipose tissue, improved insulin sensitivity and glucose metabolism, preservation of lean muscle mass, enhancement of mitochondrial function and energy expenditure, and muscle strength and recovery support. A 2024 preclinical study published in Scientific Reports demonstrated additive improvements in grip strength and exercise endurance when combined with resistance training in aged mice.
Administration
Research protocols use oral dosing of approximately 50 mg taken 1–3 times daily, or subcutaneous injection. Common research cycles are approximately 2 months on, followed by a 1-month washout period.
Potential Adverse Effects
Generally well tolerated in available studies. Reported mild effects include nausea, fatigue, and dizziness. Long-term human safety data is not established.
Properties
- Name: 5-Amino-1MQ (5-Amino-1-methylquinolinium)
- Type: Synthetic small molecule NNMT inhibitor
- Length: N/A (small molecule, not a peptide)
- Sequence: N/A
- Molecular Weight: ~175.21 Da (iodide salt form ~301.13 Da)
- Formula: C₁₀H₁₀N₂ (free base); C₁₀H₁₀N₂·HI (iodide salt)
2. Structural Properties Compound Nature: Bicyclic aromatic quinolinium cation; the quinoline ring system bears a methyl group at N-1 (generating the quaternary ammonium/quinolinium cation) and an amino group at the 5-position; the positively charged nitrogen is the defining feature of the quinolinium pharmacophore
Secondary Structure: N/A (small molecule); planar aromatic ring system enables intercalation-type stacking interactions with the NNMT active site; the 5-amino group is proposed to form hydrogen bonds within the substrate-binding pocket
Hydrophobicity: Moderately hydrophilic due to the quinolinium cation and 5-amino group; cell permeability is reported despite cationic character, attributed to the planar aromatic system facilitating membrane partitioning
Charge: Permanent positive charge on the quinolinium nitrogen at all physiological pH values; supplied as iodide or other counterion salt
3. Solubility
- Soluble in water, DMSO, and polar organic solvents; aqueous solubility reported above 10 mg/mL for the salt form
- DMSO stock solutions at 10–50 mM commonly used in cell-based research; dilute to ≤0.1% DMSO final concentration in biological assays
- Supplied as crystalline solid or powder; typically the iodide or chloride salt form
4. Stability Thermal Stability: Stable as a solid at room temperature; protect from prolonged exposure to light due to potential photodegradation of the aromatic amine; DMSO stock solutions stable at −20°C for extended periods
Metabolic Stability: Cell-permeable; reported to remain active intracellularly in preclinical cell culture models; metabolic fate in vivo not fully characterized in published literature; oral bioavailability data from preclinical rodent studies suggests moderate to good absorption
Storage: Store as solid at −20°C protected from light and moisture; DMSO solutions stable at −20°C for up to 12 months; avoid repeated freeze-thaw cycles of stock solutions
5. Chemical Reactivity Quinolinium nitrogen carries a permanent positive charge; the aromatic ring system is stable under physiological conditions and resistant to hydrolysis
The 5-amino group (aromatic amine) is susceptible to oxidation under strongly oxidative conditions; protect from peroxides and prolonged air exposure in solution
Competitive inhibition of NNMT is proposed to occur via substrate-competitive binding at the nicotinamide binding site of the enzyme active site
No reactive electrophilic groups; covalent modification of biological targets is not described in the research literature; mechanism is non-covalent competitive inhibition
Counterion (iodide or chloride) is pharmacologically inert at research concentrations
6. Other Properties
- Enzyme target: Selective inhibitor of nicotinamide N-methyltransferase (NNMT); NNMT catalyzes the SAM-dependent methylation of nicotinamide to 1-methylnicotinamide (1-MNA), consuming both nicotinamide (a NAD+ precursor) and SAM in the process
- NAD+ preservation: NNMT inhibition by 5-Amino-1MQ is reported to increase intracellular NAD+ and SAM availability in preclinical cell and animal models by redirecting nicotinamide toward the NAD+ salvage pathway
- Cell permeability: Reported as cell-permeable despite cationic character; intracellular NNMT inhibition demonstrated in cell-based assays in the published literature
- Research stage: Preclinical compound; no clinical trials registered or completed as of available literature; all bioactivity data derived from cell culture and rodent model studies
Description
5-Amino-1MQ (5-amino-1-methylquinolinium) is a synthetic research compound and has been described in the scientific literature as a selective, cell-permeable inhibitor of nicotinamide N-methyltransferase (NNMT), an enzyme involved in nicotinamide methylation and intracellular NAD+ regulation. Publications referencing 5-Amino-1MQ discuss it in the context of metabolic enzyme pharmacology, NAD+ pathway biology, and sirtuin-associated signaling within experimental systems.
Reports involving 5-Amino-1MQ describe its proposed inhibitory activity at the NNMT enzyme and associated downstream signaling properties under defined experimental conditions. Observations of NAD+ level modulation, SIRT1 pathway-associated markers, S-adenosylmethionine (SAM) availability dynamics, and mitochondrial function-associated signaling components are limited to non-clinical research settings and are reported as descriptive findings within cellular and animal model studies.
All references to 5-Amino-1MQ are confined to mechanistic and observational research contexts and do not extend beyond laboratory-based investigation.
In the scientific literature, 5-Amino-1MQ has been referenced in non-clinical research involving enzyme inhibition assays, metabolic signaling studies, and preclinical animal models. These publications describe experimental contexts in which molecular interactions, NAD+ pathway components, and metabolic signaling markers were observed and recorded.
Reported research contexts include examination of:
- NNMT enzyme inhibition dynamics and intracellular NAD+ modulation patterns in experimental models
- SIRT1 pathway-associated signaling components and mitochondrial biogenesis markers observed in research settings
- S-adenosylmethionine (SAM) availability and methylation-dependent gene expression markers evaluated under experimental conditions
- Adipose tissue metabolism and fat oxidation pathway components assessed in preclinical animal contexts
- Comparative NNMT inhibition profiles and selectivity characteristics relative to other methyltransferase inhibitors in experimental systems
All reported applications are confined to descriptive investigation within controlled laboratory research environments.
Mechanistic discussions in preclinical publications describe 5-Amino-1MQ as a quinolinium-based small molecule in which NNMT inhibition is described as preserving intracellular NAD+ by blocking the conversion of nicotinamide to 1-methylnicotinamide (1-MNA). The resulting increase in NAD+ bioavailability is discussed in the context of sirtuin activation and metabolic flexibility signaling within the cited literature. These descriptions are limited to molecular and biochemical observations within experimental systems and do not imply functional outcomes beyond the reported research context.
5-Amino-1MQ is supplied as a research-grade compound material. Identity and composition have been reported as characterized using analytical techniques commonly applied to small molecule research materials, including chromatographic and mass spectrometric methods. Individual laboratories determine handling, storage, and analytical verification parameters in accordance with internal research protocols.
COA
Storage
Lyophilization is a unique dehydration process, also known as cryodesiccation, where the peptides are frozen and then subjected to low pressure. This causes the water in the peptide vial to sublimate directly from solid to gas, leaving behind a stable, crystalline white structure known as lyophilized peptide. The puffy white powder can be stored at room temperature until you're ready to reconstitute it with bacteriostatic water.
Once peptides have been received, it is imperative that they are kept cold and away from light. If the peptides will be used immediately, or in the next several days, weeks or months, short-term refrigeration under 4°C (39°F) is generally acceptable. Lyophilized peptides are usually stable at room temperatures for several weeks or more, so if they will be utilized within weeks or months such storage is typically adequate.
For longer term storage (several months to years) it is more preferable to store peptides in a freezer at -80°C (-112°F). When storing peptides for months or even years, freezing is optimal in order to preserve the peptide's stability.