Fmoc-L-glutamic acid α-methyl ester
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Fmoc-L-glutamic acid α-methyl ester

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Category
Fmoc-Amino Acids
Catalog number
BAT-001985
CAS number
145038-49-9
Molecular Formula
C21H21NO6
Molecular Weight
383.36
IUPAC Name
(4S)-4-(9H-fluoren-9-ylmethoxycarbonylamino)-5-methoxy-5-oxopentanoic acid
Synonyms
Fmoc-L-Glu-Ome; (4S)-4-(9H-Fluoren-9-ylmethoxycarbonylamino)-5-methoxy-5-oxopentanoicacid
Appearance
White powder
Purity
≥ 99% (HPLC)
Density
1.296±0.06 g/cm3(Predicted)
Melting Point
120-140°C
Boiling Point
630.6±55.0 °C(Predicted)
Storage
Store at RT
InChI
InChI=1S/C21H21NO6/c1-27-20(25)18(10-11-19(23)24)22-21(26)28-12-17-15-8-4-2-6-13(15)14-7-3-5-9-16(14)17/h2-9,17-18H,10-12H2,1H3,(H,22,26)(H,23,24)/t18-/m0/s1
InChI Key
GVVDKFNHFXLOQY-SFHVURJKSA-N
Canonical SMILES
COC(=O)C(CCC(=O)O)NC(=O)OCC1C2=CC=CC=C2C3=CC=CC=C13

Fmoc-L-glutamic acid α-methyl ester, a versatile chemical compound utilized in peptide synthesis and amino acid research, finds diverse applications across various domains.

Peptide Synthesis: As a pivotal component in solid-phase peptide synthesis, Fmoc-L-glutamic acid α-methyl ester serves as a foundational building block. Its unique Fmoc protecting group enables selective deprotection, facilitating the incremental addition of amino acids.

Protein Engineering: Within the realm of protein engineering, Fmoc-L-glutamic acid α-methyl ester plays a crucial role in exploring protein structure-function relationships. By integrating this compound into synthetic peptides, scientists can delve into the impact of altered glutamic acid residues on protein stability and activity. This approach is instrumental in the development of proteins with enhanced properties, tailored for therapeutic or industrial use.

Drug Development: In the realm of drug discovery, Fmoc-L-glutamic acid α-methyl ester finds widespread application in creating peptide-based therapeutics. Its incorporation into peptide libraries enables researchers to screen for bioactive compounds with potential as enzyme inhibitors, receptor agonists, or signaling molecules. Leveraging the compound’s ability to mimic natural amino acids enhances the identification of lead compounds, crucial for advancing drug development.

Bioconjugation: Serving as a vital linker in bioconjugation strategies, Fmoc-L-glutamic acid α-methyl ester facilitates the connection of two molecules to form a cohesive entity with combined functionalities. Through the utilization of this compound, researchers can attach peptides to diverse cargos such as drugs, fluorophores, or nanoparticles. This approach enhances the delivery and targeting of therapeutic agents, elevating efficacy and specificity in medical applications.

1. 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.
2. 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.
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