Pubchem 5-Amino-1-Methylquinolinium
PubChem 5-amino-1-methylquinolinium references the chemical database entry for a small-molecule quinolinium derivative widely investigated as a selective inhibitor of nicotinamide N-methyltransferase (NNMT). This technical overview examines its molecular structure, enzyme kinetics, preclinical assay protocols, and rigorous quality standards for laboratory evaluation.
Quick answer
PubChem 5-amino-1-methylquinolinium references the chemical database entry for a small-molecule quinolinium derivative widely investigated as a selective inhibitor of nicotinamide N-methyltransferase (NNMT). This technical overview examines its molecular structure, enzyme kinetics, preclinical assay protocols, and rigorous quality standards for laboratory evaluation.
Key takeaways
- In chemical databases like PubChem, 5-amino-1-methylquinolinium (frequently designated as 5-amino-1-MQ) represents a membrane-impermeant or cell-permeable cationic small molecule that selectively inhibits the enzyme nicotinamide N-methyltransferase (NNMT).
- In the National Center for Biotechnology Information (NCBI) PubChem structure library, 5-amino-1-methylquinolinium is indexed under specific chemical identifiers including its unique compound identification number (CID), IUPAC designation, and precise monoisotopic mass.
- Nicotinamide N-methyltransferase is a cytosolic enzyme responsible for methylating nicotinamide using S-adenosylmethionine as the methyl donor, producing 1-methylnicotinamide (MNA) and S-adenosylhomocysteine (SAH).
- Preclinical investigations using rodent models and primary cell cultures have illuminated the role of NNMT inhibition in metabolic regulation.
Direct Definition and Chemical Identity
In chemical databases like PubChem, 5-amino-1-methylquinolinium (frequently designated as 5-amino-1-MQ) represents a membrane-impermeant or cell-permeable cationic small molecule that selectively inhibits the enzyme nicotinamide N-methyltransferase (NNMT). Supplied exclusively as a research-grade compound for in vitro and laboratory investigation, it serves as an essential tool for evaluating cellular methyl-donor availability, SAM/SAH balance, and metabolic flux.
The canonical compound entry recorded in chemical reference repositories details a quinolinium core substituted with an amino functional group at position 5 and a methyl group at position 1. This quaternary ammonium architecture grants unique interaction capabilities within the active site of NNMT. In vitro assays demonstrate that 5-amino-1-methylquinolinium functions as a competitive small-molecule inhibitor, impeding the transfer of a methyl group from S-adenosylmethionine (SAM) to nicotinamide (NAM), thereby altering downstream cellular energetics and gene expression profiling.
PubChem CID Profile and Molecular Properties
In the National Center for Biotechnology Information (NCBI) PubChem structure library, 5-amino-1-methylquinolinium is indexed under specific chemical identifiers including its unique compound identification number (CID), IUPAC designation, and precise monoisotopic mass. Researchers referencing the 5-amino-1-MQ reagent cross-check these identifiers to verify chemical purity, salt form (commonly iodized or chloride salts), and molecular formula prior to initiating quantitative assays.
The molecular structure features a bicyclic aromatic system that maintains high thermodynamic stability across standard laboratory temperatures. Because quaternary ammonium cations display distinct solubility and polar surface area profiles compared to neutral heterocycles, researchers must account for these physicochemical attributes when designing cellular culture buffers, buffer pH ranges, and analytical chromatography methodologies.
Enzymatic Target: Nicotinamide N-Methyltransferase (NNMT)
Nicotinamide N-methyltransferase is a cytosolic enzyme responsible for methylating nicotinamide using S-adenosylmethionine as the methyl donor, producing 1-methylnicotinamide (MNA) and S-adenosylhomocysteine (SAH). By consuming nicotinamide, NNMT directly impacts the salvage pathway required for nicotinamide adenine dinucleotide (NAD+) synthesis. Consequently, cellular models with elevated NNMT activity frequently exhibit depleted NAD+ pools and reduced oxidative phosphorylation capacity.
When introduced into in vitro enzyme assays, 5-amino-1-methylquinolinium blocks the substrate-binding pocket of NNMT. Preclinical studies suggest that targeted inhibition of NNMT restores intracellular NAD+ availability, increases S-adenosylmethionine concentrations, and shifts cellular metabolism toward enhanced mitochondrial respiration. Laboratories utilizing our broader catalog of research peptides and small molecules frequently employ NNMT inhibitors to map the intricate regulatory circuits connecting methylation capacity to cellular energy expenditure.
Preclinical Literature and Experimental Findings
Preclinical investigations using rodent models and primary cell cultures have illuminated the role of NNMT inhibition in metabolic regulation. In high-fat diet rodent models, administration of 5-amino-1-methylquinolinium was reported to reduce adipocyte hypertrophy, lower systemic lipogenesis, and elevate resting metabolic rate without altering food intake. These findings indicate that NNMT functions as a master metabolic regulator in adipose and liver tissues.
In vitro data further demonstrate that treating senescent or metabolically stressed cell lines with 5-amino-1-methylquinolinium increases intracellular NAD+ levels and downstream sirtuin enzyme activity. Researchers investigating NNMT inhibitor mechanisms frequently benchmark 5-amino-1-methylquinolinium against other pathway Modulators to dissect how methyl group consumption alters histone methylation patterns and epigenetic control.
Comparative Analysis: NNMT Inhibitors vs. Alternative Metabolic Regulators
Within the domain of metabolic and cellular energy research, scientists frequently evaluate multiple target pathways to compare physiological outcomes in vitro. While 5-amino-1-methylquinolinium operates via direct active-site competitive inhibition of NNMT, alternative metabolic research compounds act through distinct signaling cascades. For instance, mitochondrial-derived peptides like MOTS-c regulate metabolic homeostasis by activating AMPK and translocating to the nucleus during cellular stress, whereas growth hormone secretagogue fragments such as AOD-9604 influence lipolytic signaling pathways without directly altering methylation balance or NAD+ salvage enzymes.
Comparing these distinct mechanisms allows research teams to map complementary pathways in metabolic disease models. When evaluating small-molecule NNMT inhibitors alongside peptide regulators in the cellular energy research hub, investigators can cross-validate how direct enzyme inhibition differs from receptor-mediated signal transduction in preclinical assays.
Laboratory Handling, Reconstitution, and Storage Protocols
To preserve chemical integrity and prevent standard molecular degradation, 5-amino-1-methylquinolinium must be stored under controlled environmental conditions. The lyophilized or crystalline salt form is typically stored at -20°C in a desiccated container protected from direct light exposure. Prior to opening, vials should be allowed to equilibrate to room temperature to prevent condensation of ambient moisture on the solid compound.
Reconstitution protocols vary depending on the planned assay system. For aqueous in vitro assays, sterile laboratory-grade dimethyl sulfoxide (DMSO) or high-purity phosphate-buffered saline (PBS) may be utilized, depending on the salt counterpart. Stock solutions prepared in DMSO should be aliquoted into single-use microcentrifuge tubes and stored at -80°C to avoid repeated freeze-thaw cycles that can induce chemical breakdown over extended evaluation periods.
Analytical Verification: RP-HPLC and Mass Spectrometry
Achieving reproducible scientific data requires validated chemical purity. Every lot of 5-amino-1-methylquinolinium supplied by PX1 Research undergoes rigorous testing via Reverse-Phase High-Performance Liquid Chromatography (RP-HPLC) paired with Mass Spectrometry (MS) to verify molecular identity and purity limits exceeding standard academic requirements.
RP-HPLC analysis establishes that the compound peak exhibits absolute chromatographic purity without co-eluting organic impurities or degradation fragments. Mass spectrometry confirms the exact mass-to-charge ratio (m/z) corresponding to the 5-amino-1-methylquinolinium cation structure. Researchers reviewing lot-specific documentation can access full raw spectra provided within our public-facing certificates of analysis.
Endotoxin Control and Quality Assurance in Preclinical Models
In cell culture and preclinical rodent experiments, bacterial endotoxin contamination can confound biological measurements by triggering non-specific inflammatory signaling pathways. Standard chemical synthesis of small molecules can introduce residual solvents, heavy metals, or endotoxin contaminants if strict quality controls are omitted during post-synthesis purification steps.
PX1 Research enforces stringent endotoxin testing protocols utilizing Chromogenic Recombinant Factor C (rFC) or LAL assays for all laboratory compounds. Combined with synthesis conducted in GMP-compliant facilities and testing inside an ISO 17025 accredited laboratory environment, institutional research teams receive compounds verified free of confounding biological impurities.
Institutional Sourcing and USA Manufacturing Advantages
For universities, biotechnology firms, and institutional research facilities, supply chain reliability and lot-to-lot consistency are essential parameters. PX1 Research manufactures and inventories its research compounds within USA-based facilities located in California and Arizona, providing rapid same-day dispatch for orders finalized before standard cutoff times.
Academic laboratories and corporate R&D teams seeking high-volume requisitions or dedicated batch reservations can coordinate through our specialized wholesale account program. Every shipment includes lot-traceable analytical documentation, ensuring full compliance with institutional audit requirements and internal safety protocols.
Frequently Asked Questions
What is PubChem 5-amino-1-methylquinolinium?
It refers to the PubChem chemical database listing for 5-amino-1-methylquinolinium (5-amino-1-MQ), a small-molecule selective inhibitor of nicotinamide N-methyltransferase (NNMT) supplied strictly for in vitro and laboratory research.
What is the primary molecular target of 5-amino-1-methylquinolinium?
The primary molecular target is the cytosolic enzyme nicotinamide N-methyltransferase (NNMT), which regulates cellular methyl group transfer and NAD+ salvage pathways.
How is 5-amino-1-methylquinolinium verified for analytical purity?
Purity is verified using Reverse-Phase High-Performance Liquid Chromatography (RP-HPLC) and Mass Spectrometry (MS) to ensure correct molecular mass and minimal chemical impurities.
What solvent is recommended for reconstituting 5-amino-1-methylquinolinium?
Depending on the specific salt form and assay requirements, standard solvents include high-purity laboratory DMSO or sterile phosphate-buffered saline (PBS).
How should reconstituted stock solutions be stored in the lab?
Reconstituted stock solutions should be divided into single-use aliquots and stored at -80°C to minimize degradation from repeated freeze-thaw cycles.
Are endotoxin levels tested for PX1 Research compounds?
Yes, PX1 Research subjects compounds to validated endotoxin testing (LAL or rFC assays) to ensure suitability for sensitive cellular assays and preclinical research.
Does PX1 Research provide a lot-specific Certificate of Analysis (COA)?
Every lot supplied by PX1 Research includes a comprehensive COA featuring HPLC chromatograms, mass spectra, purity percentages, and endotoxin metrics.
Can 5-amino-1-methylquinolinium be used in human clinical trials or personal administration?
No. The compound is sold strictly as a research chemical for laboratory, in vitro, and preclinical evaluation, and is never intended for human or animal medical use.
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