5-Amino-1MQ Molecular Weight, Sequence & CAS Reference

Introduction to 5-Amino-1MQ in Preclinical Chemical Research

In modern preclinical metabolic literature, 5-Amino-1MQ (5-amino-1-methylquinolinium) occupies a distinct operational position as a targeted small-molecule enzyme inhibitor. Unlike traditional signaling peptides that interact with membrane-bound G-protein coupled receptors, 5-Amino-1MQ targets cytosolic enzyme activity. Specifically, it functions as a potent inhibitor of nicotinamide N-methyltransferase (NNMT), an enzyme heavily expressed in adipose tissue, liver, and specific tumor cell lines. Investigation into NNMT expression has expanded rapidly due to its role as a master regulator of cellular energy expenditure and methyl group availability.

Because laboratory procurement lists often categorize 5-Amino-1MQ alongside metabolic research peptides, investigators frequently request sequence data and peptide-like structural specifications. However, structural characterization demonstrates that 5-Amino-1MQ is a synthetic quinolinium derivative rather than a chain of peptide-bonded amino acids. Establishing precise physical constants—such as exact molecular mass, counterion contributions, and chemical registry identifiers—is critical for researchers preparing exact molar concentrations in cell-based assays or animal kinetic protocols. A complete inventory of operational compounds can be reviewed in our comprehensive catalog of all research peptides and chemical standards.

PX1 Research supplies high-purity research materials exclusively intended for laboratory evaluation and in vitro analytical procedures. Understanding the exact molecular weight, structural limits, and chemical properties of 5-Amino-1MQ ensures that investigative laboratories maintain rigorous protocol reproducibility across different experimental models.

Physicochemical Specifications: Molecular Mass, Formula, and CAS Reference

Accurate concentration calculations in biochemical assays require clear differentiation between the parent cation mass and the total mass of the synthesized salt. As a cationic quinolinium derivative, 5-Amino-1MQ is most commonly synthesized and isolated as an iodide or chloride salt. The fundamental chemical properties are outlined below:

Molecular Formula (Free Cation): C10H11N2+ Formula Weight (Free Cation): 159.21 g/mol Chemical Name: 5-amino-1-methylquinolin-1-ium CAS Registry Number: 42464-96-0 (5-amino-1-methylquinolinium iodide) Alternative CAS References: 132474-45-6 (unspecified salt forms / free base variations) Physical Appearance: Bright yellow to orange crystalline powder Solubility Profile: Soluble in DMSO (≥ 15 mg/mL), sparingly soluble in aqueous buffers without co-solvents

When purchasing or preparing a reference sample, such as our standardized 5-Amino-1MQ 5mg reagent, researchers must account for the molecular weight of the counterion. For the iodide salt form (C10H11IN2), the total formula weight increases to approximately 286.11 g/mol due to the inclusion of the iodide ion (126.90 g/mol). Failing to adjust for this counterion mass will lead to systematic errors in calculated molarities during in vitro enzyme inhibition assays.

Structural Analysis: Small Molecule vs. Amino Acid Sequence

A common query among comparative researchers centers on the 'amino acid sequence' of 5-Amino-1MQ. It is scientifically important to clarify that 5-Amino-1MQ possesses no amino acid sequence, primary sequence alignment, or peptide backbone. It is not an oligopeptide, nor is it synthesized via solid-phase peptide synthesis (SPPS). Instead, it is a fully synthetic aromatic small molecule derived from the quinoline ring system.

The molecular architecture consists of a bicyclic quinoline core with a methyl substitution at the nitrogen position (position 1), conferring a permanent positive charge (quinolinium cation), and an amino group substitution at position 5. This compact, planar cationic structure allows the molecule to enter the catalytic pocket of NNMT, competing directly with native methyl donors and substrates. Because there are no peptide bonds, the molecule exhibits absolute immunity to proteases, peptidases, and enzymatic cleavage pathways that typically degrade short-chain peptide compounds in biological fluids.

For laboratories building topical research clusters around metabolic regulation, distinguishing between small-molecule enzyme inhibitors and peptide-based agonists is essential. While peptides target extracellular receptors to initiate intracellular signaling cascades, 5-Amino-1MQ directly permeates cellular membranes to alter enzymatic turnover rates inside the cytosol.

Salt Forms, Counterions, and Net Active Mass Determination

In analytical chemistry, salt conversion factors are critical when preparing stock solutions from solid material. Reference materials supplied as salts contain both the active pharmaceutical/research molecule and an associated counterion (e.g., iodide, chloride, trifluoroacetate, or acetate). To calculate the net active compound content (NACC) of 5-Amino-1MQ iodide, researchers utilize the ratio of the active cation weight to the total salt molecular weight.

Specifically, the ratio is calculated as: (159.21 g/mol cation) / (286.11 g/mol salt) = 0.5564. Thus, a 10.0 mg mass of pure 5-Amino-1MQ iodide contains approximately 5.56 mg of the active 5-amino-1-methylquinolinium cation, with the remaining 4.44 mg consisting of the iodide counterion. If an experimental protocol demands a final working concentration of 10 μM active cation, the total mass weighed must be adjusted upward using this stoichiometric factor.

Where specific custom salt variations are synthesized (such as acetate or chloride counterions), the molecular weight shifts accordingly. PX1 Research details the precise salt form, net compound purity, and counterion content on every lot-specific documentation set. Researchers can verify these exact metrics prior to assay reconstitution by reviewing our public archive to download a lot-specific certificate of analysis.

Mechanism of Action: NNMT Inhibition in Cellular Energetics

The primary mechanism of 5-Amino-1MQ centers on the selective inhibition of cytosolic nicotinamide N-methyltransferase (NNMT). NNMT catalyzes the transfer of a methyl group from S-adenosylmethionine (SAM) to nicotinamide (NAM), producing 1-methylnicotinamide (MNA) and S-adenosylhomocysteine (SAH). Because MNA is cleared from the cell or excreted, high NNMT activity effectively consumes methyl groups and drains the salvage pool required to regenerate nicotinamide adenine dinucleotide (NAD+).

Preclinical studies suggest that elevated NNMT activity strongly correlates with compromised cellular respiration, reduced mitochondrial density, and accelerated adipocyte lipid storage. By selectively binding to NNMT, 5-Amino-1MQ blocks the methyl transfer reaction. In vitro data indicate that this enzyme blockade preserves intracellular SAM concentrations and halts the irreversible loss of nicotinamide, directly supporting the salvage pathway that converts NAM into NAD+ via nicotinamide phosphoribosyltransferase (NAMPT).

As intracellular NAD+ availability increases following NNMT inhibition, key NAD+-dependent enzymes—including sirtuin-1 (SIRT1) and poly(ADP-ribose) polymerases (PARPs)—demonstrate elevated signaling activity in cultured adipocytes and myocytes. Consequently, 5-Amino-1MQ serves as a pivotal chemical tool for dissecting the interplay between methyl group availability, NAD+ flux, and cellular metabolic efficiency.

Mitochondrial Output and Fat-Metabolism Research In Vitro and In Vivo

In vitro models utilizing 3T3-L1 adipocytes and primary human subcutaneous fat cells demonstrate that NNMT knockdown or pharmacological inhibition via 5-Amino-1MQ alters cellular lipid dynamics. When exposed to 5-Amino-1MQ, cultured adipocytes show a marked reduction in intracellular lipid accumulation alongside an increase in basal oxygen consumption rates (OCR). These findings point to an upregulation of mitochondrial oxidative phosphorylation within fat cells.

In rodent models of diet-induced obesity, preclinical research shows that systemically administered NNMT inhibitors promote increased energy expenditure without altering total caloric intake. Researchers observed reductions in white adipose tissue (WAT) depot mass, enhanced glucose tolerance, and elevated expression of mitochondrial markers, such as peroxisome proliferator-activated receptor gamma coactivator 1-alpha (PGC-1α) and uncoupling protein 1 (UCP1).

Furthermore, skeletal muscle tissue isolated from treated animal models exhibits increased mitochondrial density and heightened basal metabolic turnover. These collective observations make 5-Amino-1MQ a high-value tool in laboratories investigating metabolic syndrome, obesity pathogenesis, and mitochondrial biogenesis. Further background on enzymatic pathways and metabolic protocols can be accessed through our institutional research library.

Comparative Profile: 5-Amino-1MQ vs. Related Metabolic Research Compounds

To contextualize 5-Amino-1MQ within the broader landscape of preclinical metabolic regulators, researchers frequently compare its activity against mitochondrial-derived peptides, lipolytic fragments, and small-molecule nuclear receptor agonists. Key comparative agents include MOTS-c, AOD-9604, and SLU-PP-332.

While MOTS-c is a 16-amino acid mitochondrial-encoded peptide that translocates to the nucleus under metabolic stress to regulate folate and purine metabolism, 5-Amino-1MQ functions directly in the cytosol as a competitive enzyme blocker. In contrast, AOD-9604 is a C-terminal peptide fragment of human growth hormone (hGH 177-191) designed specifically to stimulate lipolysis via beta-adrenergic signaling pathways rather than altered NAD+ turnover. On the other hand, SLU-PP-332 operates as an estrogen-related receptor (ERR) agonist, targeting nuclear transcription rather than direct methyltransferase kinetics. Comparing these distinct pathways allows investigators to design multi-target in vitro assays evaluating metabolic flux from orthogonal angles.

Analytical Verification: Mass Spectrometry, HPLC, and COA Standards

Given the precise quantitative requirements of enzyme inhibition assays, batch purity and accurate identity verification are non-negotiable standards. At PX1 Research, every production lot of 5-Amino-1MQ undergoes dual-tier chemical validation using High-Performance Liquid Chromatography (HPLC) and Liquid Chromatography-Mass Spectrometry (LC-MS).

HPLC analysis confirms chemical purity by measuring the relative peak area of the 5-amino-1-methylquinolinium cation against minor synthesis byproducts or degradation peaks, ensuring a minimum baseline purity of ≥ 98.0%. LC-MS spectral analysis verifies the exact molecular ion mass-to-charge ratio (m/z = 159.1 m/z for the parent cation [M]+), confirming structural identity without ambiguity. Furthermore, all materials undergo quantitative Karl Fischer titration to establish moisture content and endotoxin testing via LAL assay protocols.

All analytical procedures are performed in independent, ISO 17025-accredited laboratory facilities. Every vial supplied by PX1 Research is backed by transparent, accessible documentation, maintaining absolute confidence for analytical and cellular testing protocols.

Reconstitution, Solubility, and Laboratory Storage Protocols

5-Amino-1MQ powder exhibits physical properties distinct from lyophylized peptide cakes. Due to its ionic, aromatic structure, it displays poor solubility in plain aqueous solutions or unbuffered saline at high concentrations. For optimal laboratory handling, the compound should first be dissolved in high-purity dimethyl sulfoxide (DMSO) to create a concentrated master stock solution (e.g., 10 mM to 50 mM).

Once fully solubilized in DMSO, stock solutions can be diluted into culture media or aqueous assay buffers, ensuring that the final organic solvent concentration remains below the tolerance threshold of the biological assay (typically < 0.1% to 0.5% v/v DMSO in cell cultures). To accurately calculate stock concentration and serial dilution volumes based on exact molecular weights and salt factors, researchers can utilize our interactive reconstitution calculator.

For long-term storage, solid 5-Amino-1MQ powder should be kept desicculated at -20°C, protected from light and ambient moisture. DMSO stock solutions should be aliquoted into single-use microcentrifuge tubes and stored at -80°C to prevent freeze-thaw degradation and solvent moisture absorption.

Sourcing Standardized 5-Amino-1MQ for Institutional Research

Reliable experimental outcomes require absolute batch-to-batch consistency and fully traceable supply chains. PX1 Research manufactures and inventories high-purity research compounds strictly within USA-based, GMP-compliant facilities. Our rigorous quality control framework guarantees that institutional laboratories receive verified, unadulterated small molecules and peptides tailored for advanced analytical workflows.

Orders placed before daily cutoff thresholds ship same-day (Monday through Friday) directly from our centralized distribution hubs located in California and Arizona. This dual-hub logistics infrastructure ensures rapid, temperature-controlled delivery to laboratories nationwide, minimizing material transport stress.

For university departments, biotechnology firms, and high-throughput screening facilities requiring larger quantitative volumes or custom packaging, we provide dedicated support and bulk pricing via our institutional wholesale portal. PX1 Research remains committed to advancing scientific inquiry by upholding the highest chemical standards in the research reagent supply sector.