126251-16-9

Usage

Uses

Used in Pharmaceutical Industry:
N-Benzyloxycarbonyl-3-(4-chlorophenyl)-D-alanine is used as a key intermediate in the synthesis of various pharmaceuticals for its ability to contribute specific structural and functional properties to the final drug molecules.
Used in Organic Synthesis:
In the field of organic synthesis, N-Benzyloxycarbonyl-3-(4-chlorophenyl)-D-alanine is utilized as a building block for creating complex organic compounds, taking advantage of its reactive sites and the protective Boc group to facilitate controlled reactions.
Used in Peptide Synthesis:
N-Benzyloxycarbonyl-3-(4-chlorophenyl)-D-alanine is employed as a protected amino acid in peptide synthesis, where the Boc group ensures the selective formation of peptide bonds without unwanted side reactions, thus enhancing the yield and purity of the desired peptides.
Used in Research and Development:
In research settings, N-Benzyloxycarbonyl-3-(4-chlorophenyl)-D-alanine is used as a model compound to study the effects of various functional groups on the reactivity and selectivity of organic reactions, contributing to the advancement of synthetic methodologies.

Upstream product

• 127862-82-2 Z-DL-Phe(4Cl)-OCH₂CF₃ 
• 134306-44-8 Z-DL-Phe(4Cl)OMe 
• 13139-17-8 N-(Benzyloxycarbonyloxy)succinimide 
• 7424-00-2 DL-Phe(4Cl) 

Relevant academic research and scientific papers

Synthesis, in vitro biological activity, hydrolytic stability and docking of new analogs of BIM-23052 containing halogenated amino acids

One of the potent somatostatin analogs, BIM-23052 (DC-23-99) d-Phe-Phe-Phe-d-Trp-Lys-Thr-Phe-Thr-NH2, has established in vitro growth hormone inhibitory activity in nM concentrations. It is also characterized by high affinity to some somatostatin receptors which are largely distributed in the cell membranes of many tumor cells. Herein, we report the synthesis of a series of analogs of BIM-23052 containing halogenated Phe residues using standard solid-phase peptide method Fmoc/OtBu-strategy. The cytotoxic effects of the compounds were tested in vitro against two human tumor cell lines—breast cancer cell line and hepatocellular cancer cell line, as well as on human non-tumorigenic epithelial cell line. Analogs containing fluoro-phenylalanines are cytotoxic in μM range, as the analog containing Phe (2-F) showed better selectivity against human hepatocellular cancer cell line. The presented study also reveals that accumulation of halogenated Phe residues does not increase the cytotoxicity according to tested cell lines. The calculated selective index reveals different mechanisms of antitumor activity of the parent compound BIM-23052 and target halogenated analogs for examined breast tumor cell lines. All peptides tested have high antitumor activity against the HepG2 cell line (IC50 ≈ 100?μM and SI > 5) compared to breast cells. This is probably due to the high permeability of the cell membrane and the higher metabolic activity of hepatocytes. In silico docking studies confirmed that all obtained analogs bind well with the somatostatin receptors with preference to ssrt3 and ssrt5. All target compounds showed high hydrolytic stability at acid and neutral pH, which mimic physiological condition in stomach and human plasma.

NOVEL OPTICALLY ACTIVE COMPOUNDS, METHOD FOR KINETIC OPTICAL RESOLUTION OF CARBOXYLIC ACID DERIVATIVES AND CATALYSTS THEREFOR

The present invention provides a method of kinetic optical resolution of carboxylic acid derivatives using specific optically active catalysts. A racemic or diastereomeric mixture of carboxylic acid derivatives of the formula (A) is reacted with a nucleophile in the presence of an optically active catalyst to form an optically active nucleophile derivative of the formula (B). The catalyst is an optically active compound represented by the formula (C) or (D) [wherein R1 is a substituted or unsubstituted, saturated or unsaturated, straight-chain, branched or alicyclic aliphatic hydrocarbon group which can have a heteroatom, R2 is ethyl or vinyl, and R5 is hydrogen or methoxy respectively].

Porcine Pancreatic Lipase Catalyzed Enantioselective Hydrolysis of Esters of N-Protected Unusual Amino Acids

Porcine pancreatic lipase catalyzed the highly enantioselective hydrolysis of a kind of α-substituted carboxylic esters, i.e., the 2,2,2-trifluoroethyl esters of the N-benzyloxycarbonyl derivatives of unusual amino acids.