1、 Overview
N-Methyl-DL-alanine is not only an important chiral source for the synthesis of chiral reagents in the field of asymmetric synthesis, but also has wide applications in pharmaceutical synthesis, racemate resolution and other fields.
2、 Basic Product Information
3、N-Methyl-DL-alanine (CAS: 600-21-5) — Q&A
Answer: There are two core differences. Common natural L-alanine is an L-configured α-amino acid with a primary amino group (—NH₂) attached to the α-carbon. In N-Methyl-DL-alanine, a methyl group is bonded to the amino nitrogen to form a secondary amine structure (—NHCH₃). It is a racemate containing equal amounts of D and L configurations and exhibits no optical activity. This structure means it is not a standard substrate for ribosomal protein synthesis and cannot participate in normal biological protein production.
In terms of chemical properties: the methyl group on nitrogen creates steric hindrance, which alters its reaction efficiency with bulky electrophiles; the nucleophilicity of the secondary amine is not inherently lower than that of a primary amine. Its acid-base dissociation parameters differ from natural alanine. Literature reference values are approximately pK₁ 2.22 and pK₂ 10.19, with minor variations across different references. Within peptide chains, N-methylation can change the conformational preference of amide bonds, eliminate backbone amide hydrogens, and reshape the molecular hydrogen-bonding pattern. The free form is hygroscopic and shall be stored in a sealed, moisture-proof environment.
Answer: This product is a racemate with equal amounts of D and L enantiomers and has no optical activity. Its core application value lies in serving as a substrate and precursor for chiral resolution. High-purity single-enantiomer N-methylalanine can be obtained via chiral resolution, providing scarce non-natural N-methyl amino acid monomers for the synthesis of chiral drugs and chiral ligands. It can also be used as a racemic intermediate: non-stereoselective synthetic reactions are carried out first, followed by resolution to produce enantiopure products. The racemate itself has no enantioselectivity and cannot be directly used for chiral catalysis or chiral ligand construction. It must be resolved into a single chiral enantiomer before it can be applied in stereoselective synthetic systems.
Answer: For targeted N-methylation modification of peptides, this product delivers modification effects that ordinary natural alanine cannot achieve. Peptides built from ordinary alanine are readily recognized and hydrolyzed by proteases in vivo, resulting in rapid metabolism and low bioavailability. After modification with N-Methyl-DL-alanine, steric hindrance from the methyl group shields protease recognition sites. Meanwhile, the absence of backbone amide hydrogens removes the hydrogen-bond network required for protease recognition, effectively improving the peptide’s resistance to hydrolysis and metabolic degradation. In certain peptide sequences, N-methyl modification can optimize molecular lipophilicity and enhance cell membrane permeability.
This modification effect is site- and density-dependent. Not all modification sites produce the desired effect, and there is no universal optimization benefit. It is only suitable for specific peptide modification requirements.
Answer: Free N-Methyl-DL-alanine has excellent water solubility. The primary purpose of salt formation is not to improve solubility, but to optimize storage stability and experimental handling performance. N-Methyl-DL-alanine hydrochloride (CAS 32012-14-9, molecular formula C₄H₁₀ClNO₂, molecular weight approx. 139.58) features better crystallinity and more stable physicochemical properties. It facilitates accurate weighing, purification and industrial application. The hygroscopicity of the product shall refer to the official SDS and measured data.
Its salt form is compatible with aqueous-phase pharmaceutical synthesis, in vitro biological activity assays, R&D of water-soluble peptide formulations and other systems. It can be directly used in some organic coupling reactions without prior neutralization of the free base, effectively broadening its application scope in aqueous-phase synthesis.
Answer: This product is a synthetic non-proteinogenic amino acid. It is not a standard substrate for ribosomal protein synthesis and will not be incorporated into biological proteins through normal translation processes. Organisms possess natural metabolic pathways for N-methyl amino acids, so this compound is not entirely devoid of metabolic routes. It can be used as a research substrate for enzyme-mediated demethylation and oxidative metabolism mechanisms.
Its core research value: it can act as a specific comparison probe to investigate the recognition, binding and transport rules of N-methylated amino acids by amino acid transporters. It can serve as a synthetic building block to prepare N-methylated peptidomimetics for studying peptide metabolic stability and membrane permeability. It also supports basic research and development of novel biomaterials such as non-natural peptides and functional peptidomimetics.
Answer: This product is a common chiral source material in asymmetric synthesis. It is a racemate containing equal amounts of D and L configurations with no optical activity, and can serve as a standard substrate for the development of chiral resolution processes. High-enantiopure single-configuration N-methylalanine can be obtained via chiral resolution, providing non-natural chiral monomer raw materials for the synthesis of chiral drugs, chiral ligands and fine chiral chemicals. Meanwhile, it can be used as a racemic synthetic intermediate: non-stereoselective organic reactions are carried out first, followed by chiral resolution to obtain high-purity enantiomeric products. This synthetic strategy is suitable for the preparation processes of various chiral pharmaceutical intermediates. The racemate itself has no enantioselectivity and cannot be directly applied in chiral catalysis or chiral ligand construction. It must be resolved into a single chiral configuration before being used in stereoselective synthetic systems.
Answer: This product is a core building block for preparing N-methylated modified peptides. N-methyl modification creates steric hindrance on the peptide backbone, hindering the recognition and binding of proteases in vivo and reducing enzymatic cleavage of peptide bonds. Meanwhile, N-methyl substitution eliminates backbone amide hydrogens of peptides and disrupts the hydrogen-bond network required for protease recognition, effectively enhancing the peptide’s resistance to protease hydrolysis and metabolic degradation. In addition, N-methyl modification can restrict intramolecular hydrogen bonds and constrain the conformational flexibility of peptide chains, optimizing lipophilicity and biomembrane permeability in some peptide sequences. Such modification effects are site- and density-dependent with no universal improvement effect. The optimal modification sites and modification density shall be screened according to the target peptide sequence.
Answer: This product is an important fine intermediate for biomedicine, mainly applied in the synthetic R&D of various non-natural peptides and drug analogues. Its single chiral configuration product obtained through chiral resolution can act as a core building block for the R&D and preparation of novel targeted drugs, peptide active molecules and immunomodulatory peptide analogues. It can also be used to synthesize research-active compounds such as antimicrobial peptides and functional peptidomimetics, extensively supporting the preliminary structural optimization, activity screening and process development of innovative drugs and generic drugs. It is a distinctive synthetic raw material in the field of peptide drug R&D.
Answer: This product is a non-proteinogenic amino acid. It is not a standard substrate for ribosomal protein synthesis and will not be incorporated into biological proteins through conventional translation mechanisms, making it an excellent tool molecule for biochemical mechanism research. It can be used to investigate the recognition, binding and transmembrane transport rules of N-methylated amino acids by cell membrane amino acid transporters. Its unique acid-base dissociation constants can improve the separation performance of N-methylated amino acids in liquid chromatography, fit the qualitative and quantitative detection of such substances, and support metabolomic analysis. Meanwhile, it can be used as a standard substrate to explore basic enzymatic mechanisms including amino acid demethylation and oxidative metabolism.
Answer: This product is a dedicated synthetic building block for fine chemical and biomedical industries. Its large-scale applications mainly focus on the custom synthesis of pharmaceutical intermediates, non-natural peptides and chiral fine chemicals. The commercial product is a high-purity white crystalline powder, available in specifications ranging from lab-scale small batches to industrial bulk quantities to meet multi-level application demands for research, pilot scale-up and mass production. The product should be stored in a sealed, dry and dark environment, and can be preserved under inert gas atmosphere to effectively prevent property changes caused by moisture absorption, high temperature and oxidation, ensuring product stability. Stable mass production is realized at the industrial end based on mature organic synthesis processes, continuously adapting to industrial application scenarios of fine chemicals and biomedicine.
5、Packaging, Storage and Transportation Requirements
Packaging
Storage
Transportation
6、 Product Manager Information
Contact information:
Contact: Sophia Li
Email: sophia@coreychem.com
