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Z-D-glutamic acid α-benzyl ester

Name: Z-D-glutamic acid α-benzyl ester
Brand: BOC Sciences
Rating: 5 (1 reviews)

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

Category

CBZ-Amino Acids

Catalog number

BAT-003285

CAS number

65706-99-2

Molecular Formula

C20H21NO6

Molecular Weight

371.40

IUPAC Name

(4R)-5-oxo-5-phenylmethoxy-4-(phenylmethoxycarbonylamino)pentanoic acid

Synonyms

Z-D-Glu-Obzl; (R)-5-(Benzyloxy)-4-(((Benzyloxy)Carbonyl)Amino)-5-Oxopentanoic Acid

Appearance

White to off-white powder

Purity

≥ 98% (HPLC)

Density

1.268 g/cm3

Melting Point

95-105 °C

Boiling Point

594.3°C

Storage

Store at 2-8 °C

InChI

InChI=1S/C20H21NO6/c22-18(23)12-11-17(19(24)26-13-15-7-3-1-4-8-15)21-20(25)27-14-16-9-5-2-6-10-16/h1-10,17H,11-14H2,(H,21,25)(H,22,23)/t17-/m1/s1

InChI Key

VWHKODOUMSMUAF-QGZVFWFLSA-N

Canonical SMILES

C1=CC=C(C=C1)COC(=O)C(CCC(=O)O)NC(=O)OCC2=CC=CC=C2

Z-D-glutamic acid α-benzyl ester, a versatile chemical compound with applications across scientific disciplines, is utilized in diverse ways. Here are four key applications:

Peptide Synthesis: Integrating Z-D-glutamic acid α-benzyl ester as a protected amino acid in peptide synthesis is a common practice. The compound’s ester group acts as a pivotal protecting group for the carboxyl function during synthesis, facilitating selective reactions with other functional groups. This strategic usage is fundamental in synthesizing peptides crucial for pharmaceutical research and therapeutic innovation.

Pharmaceutical Intermediate: Serving as a vital intermediate in drug development, Z-D-glutamic acid α-benzyl ester plays a crucial role in crafting drugs and active pharmaceutical ingredients. Through subsequent chemical modifications, this compound can metamorphose into various pharmacologically active molecules. Its significance as an intermediate is prominent in the manufacturing process of specific medications, particularly those targeting distinct proteins or pathways.

Chiral Building Block: Z-D-glutamic acid α-benzyl ester emerges as a significant chiral building block in organic synthesis due to its stereochemistry. This property allows for the creation of enantioselective compounds imperative in synthesizing chiral drugs and other biologically active molecules. The use of such chiral intermediates empowers chemists to design molecules with desired properties, enhancing the efficacy and selectivity of pharmaceutical agents.

Research in Enzyme Function: In the realm of enzymatic studies, Z-D-glutamic acid α-benzyl ester becomes a valuable tool for investigating the specificity and activity of proteases and other enzymes. Whether employed as a substrate or inhibitor, researchers can delve into enzyme-substrate interactions, shedding light on enzyme function. This research is particularly significant in disciplines like biochemistry and molecular biology, where comprehending enzyme mechanisms is pivotal for advancing drug discovery and development.

1. Catalytic Asymmetric Benzylation of Azomethine Ylides Enabled by Synergistic Lewis Acid/Palladium Catalysis

Xin Chang, Jing-Di Ran, Xue-Tao Liu, Chun-Jiang Wang Org Lett. 2022 Apr 8;24(13):2573-2578. doi: 10.1021/acs.orglett.2c00865. Epub 2022 Mar 29.

The synergistic chiral Lewis acid/achiral Pd catalyst system was successfully applied in the enantioselective benzylation of various imine esters, giving a range of α-benzyl-substituted α-amino acid derivatives in satisfactory yield with excellent enantioselectivity. It is worth noting that this strategy exhibits good tolerance for bicyclic and monocyclic benzylic electrophiles. Furthermore, the utility of this synthetic protocol was demonstrated by the expedient preparation of enantioenriched antihypertensive drug α-methyl-l-dopa.

2. Catalytic asymmetric Tsuji-Trost α-benzylation reaction of N-unprotected amino acids and benzyl alcohol derivatives

Jian-Hua Liu, Wei Wen, Jian Liao, Qi-Wen Shen, Yao Lin, Zhu-Lian Wu, Tian Cai, Qi-Xiang Guo Nat Commun. 2022 May 6;13(1):2509. doi: 10.1038/s41467-022-30277-9.

Catalytic asymmetric Tsuji-Trost benzylation is a promising strategy for the preparation of chiral benzylic compounds. However, only a few such transformations with both good yields and enantioselectivities have been achieved since this reaction was first reported in 1992, and its use in current organic synthesis is restricted. In this work, we use N-unprotected amino acid esters as nucleophiles in reactions with benzyl alcohol derivatives. A ternary catalyst comprising a chiral aldehyde, a palladium species, and a Lewis acid is used to promote the reaction. Both mono- and polycyclic benzyl alcohols are excellent benzylation reagents. Various unnatural optically active α-benzyl amino acids are produced in good-to-excellent yields and with good-to-excellent enantioselectivities. This catalytic asymmetric method is used for the formal synthesis of two somatostatin mimetics and the proposed structure of natural product hypoestestatin 1. A mechanism that plausibly explains the stereoselective control is proposed.

3. Modification of the vitamin K-dependent carboxylase assay

S Romiti, W K Kappel J Biochem Biophys Methods. 1985 May;11(1):59-68. doi: 10.1016/0165-022x(85)90041-7.

Methods are presented that describe alternative protocols for the isolation of rat liver microsomes containing the vitamin K-dependent carboxylase and the procedure in which the solubilized enzyme is assayed. The method for determining the rate of 14CO2 incorporation into low molecular weight, acid soluble substrates by the rat liver microsomal vitamin K-dependent carboxylase has been modified in order to optimize safety, accuracy and simplicity. For these studies the rat liver microsomes containing the vitamin K-dependent carboxylase were isolated by CaCl2 precipitation. These Triton X-100 solubilized microsomes were found to be equivalent to the microsomes obtained by high speed ultracentrifugation with regard to protein concentration, pentapeptide carboxylase activity, carboxylase activity, preprothrombin concentration and total carboxylatable endogenous protein substrate. This modified assay procedure requires fewer steps and pipetting transfers and is quantitatively equivalent to previously employed protocols. The described technique can be adapted for any assay where 14CO2 or H14CO3- is incorporated into non-volatile products. This newly developed assay procedure was employed to assess conditions necessary for optimal vitamin K-dependent carboxylation of the less expensive substrate, N-t-Boc-L-glutamic acid alpha-benzyl ester. The optimal conditions for the carboxylation of N-t-Boc-L-glutamic acid alpha-benzyl ester by the carboxylase were found to be 10 mM N-t-Boc-L-glutamic acid alpha-benzyl ester, 10 mM MgCl2 at 15-18 degrees C. The rate of N-t-Boc-L-glutamic acid alpha-benzyl ester carboxylation under these optimized conditions was found to be higher (1.5-fold) than the rate of carboxylation of 1 mM Phe-Leu-Glu-Glu-Ile in the presence of the cation activator, MgCl2.