PROMO!
First order? Get 10% OFF with this code: 1storder
5-Amino-1-methylquinolinium (5-amino-1MQ) is a small synthetic molecule based on quinolinium which, in preclinical studies, has been found to inhibit the enzyme nicotinamide N-methyltransferase (NNMT) and is used in experimental research to study the biochemical pathways associated with NNMT and nicotinamide metabolism.
5-Amino-1MQ is a synthetic small-molecule research chemical that belongs to the nicotinamide N-methyltransferase (NNMT) inhibitor quinolinium class. In contrast to peptide-based research chemicals, 5-Amino-1MQ is a low-molecular-weight organic molecule intended for experimental study of enzyme pathways related to methylation and cellular metabolism. Its substituted quinolinium core, which is part of its chemical structure, allows for selective interaction with NNMT within a laboratory setting.
The compound was developed as part of continuing research into the biological role of NNMT, an enzyme involved in nicotinamide metabolism and the regulation of methyl donor utilisation. Since its initial characterisation in the scientific literature, 5-Amino-1MQ has become a recognised research tool for investigating enzyme activity, metabolic signalling and cellular biochemical pathways in preclinical models. Experimental studies have primarily utilised in vitro systems and animal models to examine its biochemical dynamics and pharmacological characteristics.
5-Amino-1MQ lacks an advanced secondary structure and primary amino acid sequence since it is a synthetic, low-molecular-weight quinolinium derivative rather than a peptide. Rather, the molecule's chemical structure is a well-defined aromatic heterocyclic framework made up of a substituted quinolinium ring system with an amino functional group and a permanently charged quaternary nitrogen atom. Its comparatively small structure sets it apart from bulkier peptide-based research compounds and helps explain its consistent chemical behavior in the lab.
The compound's physicochemical characteristics, such as its water solubility and chromatographic behavior, are influenced by the quaternary ammonium centre, which confers a permanent positive charge over a wide physiological pH range. For research purposes, 5-Amino-1MQ is typically supplied as a water-soluble salt that makes it easier to prepare analytical standards and experimental solutions. A certain amount of structural stiffness is also provided by the aromatic ring, and the amino substituent provides a site for intermolecular interactions important for biological studies.
As a fully synthetic molecule, 5-Amino-1MQ does not contain post-translational modifications or peptide-specific structural features such as cyclization, amidation or disulphide bridges. Under recommended laboratory storage conditions, the dry compound demonstrates good chemical stability, although, like many organic research chemicals, it should be protected from excessive moisture, prolonged light exposure and elevated temperatures to minimise degradation. Its identity and physical integrity are routinely confirmed using analytical techniques including high-performance liquid chromatography (HPLC), liquid chromatography–mass spectrometry (LC-MS) and, where appropriate, nuclear magnetic resonance (NMR) spectroscopy.
Nicotinamide N-methyltransferase (NNMT), a cytosolic enzyme that methylates nicotinamide using S-adenosyl-L-methionine (SAM) as the methyl donor, has been selectively inhibited by 5-Amino-1MQ in laboratory settings. Existing published experimental research indicates that the material interacts with the catalytic site of NNMT, where enzyme inhibition has been characterized by biochemical and structural investigations.
In vitro studies have examined how NNMT inhibition affects intracellular metabolic pathways associated with methyl-donor usage and nicotinamide metabolism. Experimental research on changes in nicotinamide conversion to 1-methylnicotinamide (1-MNA) has shed light on the enzyme's role in larger metabolic networks. These investigations have also found changes in metabolites linked to the nicotinamide adenine dinucleotide (NAD⁺) salvage pathway; however, the precise downstream effects are still being investigated.
Published studies have further examined the relationship between NNMT activity and cellular methylation capacity. As NNMT consumes SAM during catalysis, laboratory investigations have explored how enzyme inhibition may influence the intracellular availability of methyl donors and associated one-carbon metabolic pathways. These interactions have been characterised using enzymatic assays, metabolomic profiling and molecular biological techniques.
At the cellular level, experimental models have investigated signaling networks associated with NNMT activity, including pathways involved in cellular energy metabolism, gene regulation, and cellular differentiation. Research has also examined transcriptional regulation of NNMT expression throughout different tissue types to better understand the biological context in which the enzyme is expressed.
The mechanism of 5-Amino-1MQ continues to be characterised through in vitro biochemical assays, structural biology and preclinical experimental models. Current evidence indicates that its primary molecular interaction is selective inhibition of NNMT, in ongoing research examining the effects on intracellular metabolic pathways and enzyme-regulated biochemical processes.
The findings summarized here are based on published preclinical and in vitro studies. Primary research sources are provided in the references.
Cellular biology studies have examined 5-Amino-1MQ as a research tool to investigate nicotinamide N-methyltransferase (NNMT) activity in cultured cells. In vitro models have been used to characterize enzyme localization, intracellular metabolic functions and biochemical activities associated with NNMT inhibition under controlled laboratory conditions.
Published molecular biology research has utilized 5-Amino-1MQ to investigate gene expression, enzyme regulation and molecular signaling associated with NNMT. Experimental approaches have included transcriptomic analysis, quantitative PCR, Western blotting and metabolomic profiling to characterize changes in molecular pathways following selective enzyme inhibition.
Neuroscience research has examined the expression and function of NNMT within the central nervous system using cellular and preclinical models. Laboratory investigations have explored the distribution of the enzyme in neural tissues and have characterised metabolic pathways associated with nicotinamide metabolism in experimental neurological research.
NNMT has been studied within larger metabolic and endocrine regulation networks in experimental endocrinology. Enzyme expression in metabolically active tissues has been studied, and linkages between NNMT activity and biochemical pathways concerned in cellular metabolism and energy homeostasis have been described.
Metabolic research represents one of the principal areas in which 5-Amino-1MQ has been investigated. Published studies have utilised biochemical assays, metabolomics and isotope-tracing techniques to characterise nicotinamide metabolism, methyl donor utilisation and intracellular metabolic flux associated with NNMT inhibition in preclinical models.
Using pure enzyme systems and structural analysis, biochemical research has concentrated on characterizing the interaction between 5-Amino-1MQ and NNMT. Enzyme kinetics, inhibition tests, crystallographic investigations, and computer modeling have all been used in experiments to study biomolecular interactions, catalytic activity, and binding properties.
5-Amino-1MQ is not produced using Solid Phase Peptide Synthesis (SPPS) since it is a synthetic small molecule rather than a peptide. Rather, it is made via traditional organic synthesis, then its chemical identity and content are confirmed through purification and analytical verification. In order to eliminate leftover starting materials, reaction byproducts, and other process-related contaminants, the molecule is usually processed using chromatographic techniques after synthesis.
Analytical high-performance liquid chromatography (HPLC) is widely used to determine chemical purity and assess batch consistency. Conversely, liquid chromatography–mass spectrometry (LC–MS) is used to confirm chemical identity and predicted molecular mass. Additional structural analysis may be performed using methods such as nuclear magnetic resonance (NMR) spectroscopy.
Prior to being made available for use in research, identity verification and purity assessment are common quality control procedures. To ensure consistency across production batches, batch-specific testing is conducted, and the analytical findings are documented in a Certificate of Analysis (CoA). This documentation, which offers verifiable quality assurance, usually consists of purity data for laboratory research, analytical test results, and batch identification.
5-Amino-1MQ capsules are supplied in a prepared capsule form for research and laboratory use. No reconstitution is required.
Store 5-Amino-1MQ capsules under the specified storage conditions and keep them dry and protected from excessive heat. Follow the documented storage conditions to maintain product quality during storage.
Nicotinamide and 5-Amino-1MQ are chemically diverse substances that play various roles in biochemical studies. One naturally occurring form of vitamin B3 is nicotinamide. While 5-Amino-1MQ is a synthetic small-molecule inhibitor created to study nicotinamide N-methyltransferase (NNMT), it functions as a precursor in the formation of nicotinamide adenine dinucleotide (NAD⁺). Rather than serving as a metabolic precursor in and of itself, 5-Amino-1MQ has been employed in lab investigations to investigate the enzymatic conversion of nicotinamide.
5-Amino-1MQ is a synthetic small molecule and is not classified as a peptide. Its molecular structure contains no peptide bonds or conventional amino acid chain. Instead, it consists of a substituted quinolinium heterocycle. Although it is frequently discussed alongside peptide research compounds, its chemical structure and method of synthesis are fundamentally different.
Because it catalyzes the methylation of nicotinamide using S-adenosyl-L-methionine (SAM) as the methyl donor, NNMT is regarded as a crucial metabolic enzyme. This reaction connects one-carbon metabolism, cellular methylation, and nicotinamide metabolism. As a result, NNMT has been thoroughly studied as part of larger research looking at enzyme function and metabolic control.
NNMT catalyses the transfer of a methyl group from SAM to nicotinamide, producing 1-methylnicotinamide (1-MNA) and S-adenosyl-L-homocysteine (SAH). This reaction represents one pathway for nicotinamide metabolism and has been examined in relation to intracellular methyl donor utilisation and NAD⁺ precursor metabolism. Experimental studies continue to investigate how NNMT integrates within these interconnected biochemical pathways.
Published biochemical studies have characterised 5-Amino-1MQ as a selective inhibitor of NNMT. Enzyme inhibition assays and structural investigations have demonstrated preferential interaction with the NNMT catalytic site, although selectivity is typically evaluated experimentally against panels of related enzymes. Ongoing research continues to characterise its specificity under different laboratory conditions.
NNMT inhibition is commonly investigated using enzyme kinetics assays, cultured cell experiments and metabolomic analyses. Additional techniques include high-performance liquid chromatography (HPLC), liquid chromatography–mass spectrometry (LC-MS), molecular docking, X-ray crystallography and gene expression analysis. These complementary methodologies enable researchers to characterise enzyme activity, inhibitor binding and downstream biochemical changes.
5-Amino-1MQ is a substituted quinolinium derivative containing an aromatic heterocyclic ring system with an amino functional group and a quaternary nitrogen atom. This permanently charged nitrogen distinguishes the molecule from many neutral organic compounds and contributes to its physicochemical properties. Its structure has been characterised using analytical techniques including LC-MS and nuclear magnetic resonance (NMR) spectroscopy.
Indeed. 5-Amino-1MQ has been widely used in published research in in vitro experimental setups, such as pure enzyme tests and cultivated cell lines. Under carefully regulated experimental circumstances, these lab models have been used to study intracellular metabolic pathways, NNMT inhibition, and enzyme kinetics.
Research involving 5-Amino-1MQ has included purified biochemical systems, cultured mammalian cells and animal models. These preclinical approaches have been used to investigate the compound’s pharmacological characteristics, enzyme inhibition and metabolic interactions. The majority of published work has focused on laboratory-based and preclinical experimental models rather than clinical investigation.
During manufacturing, standardized quality control processes are used to verify batch-to-batch uniformity. While LC-MS verifies molecular identification and anticipated molecular mass, analytical HPLC is used to evaluate chemical purity. A Certificate of Analysis (CoA), which offers traceable records of purity, identification, and quality testing for every production lot, contains batch-specific analytical results.
5-Amino-1MQ is supplied solely for laboratory research and analytical purposes. It is not intended for human or veterinary use, consumption, diagnosis, treatment, or any clinical application. Information provided on this page is for scientific reference only and should be considered alongside the cited primary literature and relevant analytical documentation.
