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L-Aspartic acid α-methyl ester

* Please kindly note that our products are not to be used for therapeutic purposes and cannot be sold to patients.

Aspartic acid α-methyl ester is a derivative of L-Aspartic Acid, a non-essential amino acid found in food sources and dietary supplements. L-Aspartic Acid is one of the 20 proteinogenic amino acids; the building blocks of proteins. Its conjugate base L-aspartate is an excitatory neurotransmitter in the central nervous system.

Category

β−Amino Acids

Catalog number

BAT-004228

CAS number

17812-32-7

Molecular Formula

C5H9NO4

Molecular Weight

147.10

IUPAC Name

(3S)-3-amino-4-methoxy-4-oxobutanoic acid

Synonyms

L-Asp-OMe; H-Asp-OMe; 1-Methyl L-Aspartate; L-Aspartic Acid 1-Methyl Ester; (S)-3-Amino-4-methoxy-4-oxobutanoic acid

Appearance

White powder

Purity

≥ 99% (TLC)

Density

1.299±0.06 g/cm3

Melting Point

186 °C

Boiling Point

272.7±30.0 °C

Storage

Store at 2-8 °C

InChI

InChI=1S/C5H9NO4/c1-10-5(9)3(6)2-4(7)8/h3H,2,6H2,1H3,(H,7,8)/t3-/m0/s1

InChI Key

SWWBMHIMADRNIK-VKHMYHEASA-N

Canonical SMILES

COC(=O)C(CC(=O)O)N

L-Aspartic acid α-methyl ester, a derivative of the amino acid L-Aspartic acid, exhibits versatility across multiple fields. Here are four key applications of L-Aspartic acid α-methyl ester:

Pharmaceutical Synthesis: Serving as a pivotal foundational component in pharmaceutical synthesis, L-Aspartic acid α-methyl ester plays a crucial role in crafting pharmaceutical compounds. Its utility extends to the production of peptide-based drugs and various therapeutic agents. This ester form enhances the stability and solubility of the compound, offering significant advantages during drug formulation processes.

Biochemical Research: Within the realm of biochemical research, L-Aspartic acid α-methyl ester serves as a primary substrate for investigating enzymatic activities. Researchers leverage this compound to delve into the functionalities of enzymes that interact with derivatives of aspartic acid. These investigations contribute to a deeper comprehension of enzymatic mechanisms and intricate metabolic pathways, expanding our knowledge at the molecular level.

Flavor and Fragrance Industry: At the forefront of the flavor and fragrance sector, L-Aspartic acid α-methyl ester emerges as a crucial intermediate in the creation of synthetic flavorings and scents. By aiding in the synthesis of complex aromatic compounds, it enhances the sensory appeal of food products and perfumes. This augmentation of sensory attributes elevates the allure of consumer goods, making them more enticing and memorable.

Nutritional Supplements: Emanating as a derivative of an essential amino acid, L-Aspartic acid α-methyl ester finds its place in dietary supplements geared towards supporting diverse metabolic functions. Its role in facilitating protein synthesis and offering a stable, easily absorbable form of amino acid renders it invaluable in the realms of sports nutrition and general health supplements. This application underscores its significance in promoting overall well-being and performance optimization.

1.Synthesis of a precursor tripeptide Z-Asp-Val-Tyr-OH of thymopentin by chemo-enzymatic method.

Zheng K1, Zhan R, Hong Y, Li J, Shi W, Li S. Prep Biochem Biotechnol. 2012;42(6):520-34. doi: 10.1080/10826068.2012.660902.

The precursor tripeptide of thymopentin was synthesized by a combination of chemical and enzymatic methods. First, Val-Tyr-OH dipeptide was synthesized by a novel chemical method in two steps involving preparation of NCA-Val. Second, the linkage of the third amino acid Z-Asp-OMe to Val-Tyr-OH was completed by an enzymatic method under kinetic control. An industrial alkaline protease alcalase was used in water-organic cosolvent systems. The synthesis reaction conditions were optimized by examining the effects of several factors including organic solvents, water content, temperature, pH, and reaction time on the yield of Z-Asp-Val-Tyr-OH. The optimum condition is of pH 10.0, 35°C, acetonitrile/Na₂CO₃-NaHCO₃ buffer system (85:15, v/v), and reaction time of 2.5 hr, which achieves tripeptide yield of more than 70%.

2.Protease-catalyzed synthesis of a precursor dipeptide, Z-Asp-Val-NH2 of thymopentin, in organic solvents.

Li SJ1, Wang JA, Xu L, Zhang XZ, Li J, Suo D. Prep Biochem Biotechnol. 2008;38(4):334-47. doi: 10.1080/10826060802325402.

The protease-catalyzed, kinetically controlled synthesis of a precursor dipeptide, Z-Asp-Val-NH(2) of thymopentin (TP-5), in organic solvents was studied. Z-Asp-OMe and Val-NH(2) were used as the acyl donor and the nucleophile, respectively. An industrial alkaline protease alcalase was used to catalyze the synthesis of the target dipeptide in water-organic cosolvent systems. The conditions of the synthesis reaction were optimized by examining the effects of several factors, including organic solvents, water content, temperature, pH, and reaction time on the yield of Z-Asp-Val-NH(2). The optimum conditions using alcalase as the catalyst are pH 10.0, 35 degrees C, in acetonitrile/Na(2)CO(3)-NaHCO(3) buffer system (9:1, V/V), reaction time 5 h, with a yield of 63%. The dipeptide product was confirmed by LC- MS.