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Application Area

Fmoc-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.

Category

Fmoc-Amino Acids

Catalog number

BAT-007669

CAS number

145038-52-4

Molecular Formula

C20H19NO6

Molecular Weight

369.37

IUPAC Name

(3S)-3-(9H-fluoren-9-ylmethoxycarbonylamino)-4-methoxy-4-oxobutanoic acid

Synonyms

Fmoc-L-Asp-OMe; Fmoc-Asp-OMe; (S)-3-((((9H-Fluoren-9-yl)methoxy)carbonyl)amino)-4-methoxy-4-oxobutanoic acid; N-Fmoc-L-aspartic Acid Methyl Ester; N-(9H-Fluorene-9-ylmethoxycarbonyl)-L-aspartic acid 1-methyl ester; Fmoc L Asp OMe; Fmoc Asp OMe;(3S)-3-(9H-fluoren-9-ylmethoxycarbonylamino)-4-methoxy-4-oxobutanoic acid

Appearance

White powder

Purity

≥ 98% (HPLC)

Density

1.322±0.06 g/cm3 (20 °C 760 Torr)

Melting Point

150-165 °C

Boiling Point

609.7±55.0 °C (Predicted)

Storage

Store at RT

InChI

InChI=1S/C20H19NO6/c1-26-19(24)17(10-18(22)23)21-20(25)27-11-16-14-8-4-2-6-12(14)13-7-3-5-9-15(13)16/h2-9,16-17H,10-11H2,1H3,(H,21,25)(H,22,23)/t17-/m0/s1

InChI Key

UEUZUMRMWJUEMK-KRWDZBQOSA-N

Canonical SMILES

COC(=O)C(CC(=O)O)NC(=O)OCC1C2=CC=CC=C2C3=CC=CC=C13

Fmoc-L-aspartic acid α-methyl ester, a derivative of protected amino acid, finds wide applications in peptide synthesis and biochemical research. Here are four key applications of Fmoc-L-aspartic acid α-methyl ester:

Peptide Synthesis: Acting as a cornerstone in solid-phase peptide synthesis (SPPS), Fmoc-L-aspartic acid α-methyl ester serves as a fundamental building block. Its Fmoc protective group, delicately removable under mild conditions, streamlines the sequential construction of peptides. This compound plays a pivotal role in ensuring the precise sequence specificity and purity of synthesized peptides, optimizing the synthesis process.

Drug Development: Within the realm of pharmaceutical exploration, Fmoc-L-aspartic acid α-methyl ester stands as a crucial ingredient in the creation of peptide-based drug candidates. Researchers seamlessly integrate this derivative into peptide chains to yield compounds with potential therapeutic properties. Its incorporation facilitates the generation of peptides featuring tailored modifications, thereby enhancing their stability and bioactivity for therapeutic efficacy.

Protein Engineering: In the pursuit of protein engineering advancements, Fmoc-L-aspartic acid α-methyl ester emerges as a key player in introducing site-specific modifications. Scientists leverage this derivative to manipulate the structural and functional characteristics of proteins, unlocking new avenues for research. This application proves instrumental in investigating protein interactions, stability, and crafting proteins with innovative functionalities to expand the horizon of protein-based technologies.

Bioconjugation: Embracing bioconjugation methodologies, Fmoc-L-aspartic acid α-methyl ester enables the seamless attachment of peptides to diverse molecules or surfaces. Peptides synthesized using this ester can be affixed to biomolecules, nanoparticles, or solid supports for the development of biosensors, diagnostic tools, or therapeutic agents. This strategy amplifies the versatility and application spectrum of peptide-based technologies, empowering advancements in bioconjugation research and application.

1. Microbial/enzymatic synthesis of chiral drug intermediates

R N Patel Adv Appl Microbiol. 2000;47:33-78. doi: 10.1016/s0065-2164(00)47001-2.

Biocatalytic processes were used to prepare chiral intermediates for pharmaceuticals. These include the following processes. Enzymatic synthesis of [4S-(4a,7a,10ab)]1-octahydro-5-oxo-4-[[(phenylmethoxy) carbonyl]amino]-7H-pyrido-[2,1-b] [1,3]thiazepine-7-carboxylic acid methyl ester (BMS-199541-01), a key chiral intermediate for synthesis of a new vasopeptidase inhibitor. Enzymatic oxidation of the epsilon-amino group of lysine in dipeptide dimer N2-[N[[(phenylmethoxy)carbonyl] L-homocysteinyl] L-lysine)1,1-disulfide (BMS-201391-01) to produce BMS-199541-01 using a novel L-lysine epsilon-aminotransferase from S. paucimobilis SC16113 was demonstrated. This enzyme was overexpressed in E. coli, and a process was developed using recombinant enzyme. The aminotransferase reaction required alpha-ketoglutarate as the amine acceptor. Glutamate formed during this reaction was recycled back to alpha-ketoglutarate by glutamate oxidase from S. noursei SC6007. Synthesis and enzymatic conversion of 2-keto-6-hydroxyhexanoic acid 5 to L-6-hydroxy norleucine 4 was demonstrated by reductive amination using beef liver glutamate dehydrogenase. To avoid the lengthy chemical synthesis of ketoacid 5, a second route was developed to prepare the ketoacid by treatment of racemic 6-hydroxy norleucine (readily available from hydrolysis of 5-(4-hydroxybutyl) hydantoin, 6) with D-amino acid oxidase from porcine kidney or T. variabilis followed by reductive amination to convert the mixture to L-6-hydroxynorleucine in 98% yield and 99% enantiomeric excess. Enzymatic synthesis of (S)-2-amino-5-(1,3-dioxolan-2-yl)-pentanoic acid (allysine ethylene acetal, 7), one of three building blocks used for synthesis of a vasopeptidase inhibitor, was demonstrated using phenylalanine dehydrogenase from T. intermedius. The reaction requires ammonia and NADH. NAD produced during the reaction was recycled to NADH by oxidation of formate to CO2 using formate dehydrogenase.

2. Catalytic asymmetric synthesis of α-methyl-p-boronophenylalanine

Shingo Harada, Ryota Kajihara, Risa Muramoto, Promsuk Jutabha, Naohiko Anzai, Tetsuhiro Nemoto Bioorg Med Chem Lett. 2018 Jun 1;28(10):1915-1918. doi: 10.1016/j.bmcl.2018.03.075. Epub 2018 Mar 28.

p-Boronophenylalanine (l-BPA) is applied in clinical settings as a boron carrier for boron neutron capture therapy (BNCT) to cure malignant melanomas. Structural modification or derivatization of l-BPA, however, to improve its uptake efficiency into tumor cells has scarcely been investigated. We successfully synthesized (S)-2-amino-3-(4-boronophenyl)-2-methylpropanoic acid in enantioenriched form as a novel candidate molecule for BNCT. Key steps to enhance the efficiency of this synthesis were enantioselective alkylation of N-protected alanine tert-butyl ester with a Maruoka catalyst and Miyaura borylation reaction to install the boron functionality.