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Fmoc-L-aspartic acid α-benzyl 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-003739

CAS number

86060-83-5

Molecular Formula

C26H23NO6

Molecular Weight

445.48

IUPAC Name

(3S)-3-(9H-fluoren-9-ylmethoxycarbonylamino)-4-oxo-4-phenylmethoxybutanoic acid

Synonyms

Fmoc-L-Asp-OBzl; Fmoc-Asp-Obzl; Fmoc-L-Aspartic acid a-benzyl ester; Fmoc-L-Aspartic alpha-benzyl ester; 1-benzyl N-fluoren-9-ylmethoxycarbonyl-L-aspartate; Fmoc-L-Asparticacid-1-benzylester

Appearance

White solid

Purity

≥ 99% (HPLC)

Density

1.310±0.06 g/cm3

Boiling Point

683.7±55.0 °C

Storage

Store at 2-8 °C

InChI

InChI=1S/C26H23NO6/c28-24(29)14-23(25(30)32-15-17-8-2-1-3-9-17)27-26(31)33-16-22-20-12-6-4-10-18(20)19-11-5-7-13-21(19)22/h1-13,22-23H,14-16H2,(H,27,31)(H,28,29)/t23-/m0/s1

InChI Key

CBZSVHFNEMONDZ-QHCPKHFHSA-N

Canonical SMILES

C1=CC=C(C=C1)COC(=O)C(CC(=O)O)NC(=O)OCC2C3=CC=CC=C3C4=CC=CC=C24

Fmoc-L-aspartic acid α-benzyl ester, a versatile chemical compound, plays a pivotal role in peptide synthesis and various advanced biochemical applications. Here are four key applications of this compound, presented with high perplexity and burstiness:

Peptide Synthesis: Serving as a cornerstone in solid-phase peptide synthesis, Fmoc-L-aspartic acid α-benzyl ester acts as a vital building block. It offers a shielded form of aspartic acid, allowing for selective deprotection during the synthesis process. This precision ensures the accurate integration of aspartic acid residues into peptide chains, a critical step in the creation of customized peptides for both research and therapeutic purposes.

Drug Development: Positioned at the forefront of pharmaceutical innovation, this compound finds extensive utility in developing peptide-based drugs. By facilitating the generation of peptide analogs and derivatives, researchers can explore novel drug candidates with heightened efficacy and reduced side effects. The ability to finely tune peptide sequences is invaluable in crafting specialized medications that target specific proteins or biological pathways.

Bioconjugation: Embracing the realm of bioconjugation, Fmoc-L-aspartic acid α-benzyl ester contributes to linking peptides with various molecules, such as fluorophores, drugs, or nanoparticles. This conjugation process enhances key properties of peptides, including stability, solubility, and targeting capabilities. These peptide conjugates find application across a spectrum of uses, spanning from in vivo imaging to targeted drug delivery and diagnostic assays.

Structure-Activity Relationship (SAR) Studies: In the domain of structure-activity relationship investigations, Fmoc-L-aspartic acid α-benzyl ester stands as a fundamental tool for synthesizing peptides with deliberate variations. Through strategic alterations in peptide sequences at specific sites, scientists can probe the intricate relationship between a peptide’s structure and its biological activity. This knowledge is paramount in designing peptides tailored to exhibit desired biological properties for both therapeutic interventions and research endeavors.

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. 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.

3. 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.

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