127888-10-2

Basic information

• Product Name: N-Benzyloxycarbonyl-3-(4-chlorophenyl)-L-alanine
• Synonyms: N-Benzyloxycarbonyl-3-(4-chlorophenyl)-L-alanine;(S)-2-(((Benzyloxy)carbonyl)aMino)-3-(4-chlorophenyl)propanoic acid
• CAS NO: 127888-10-2
• Molecular Formula: C₁₇H₁₆ClNO₄
• Molecular Weight: 333.77
• Mol File: 127888-10-2.mol
• Article Data: 4

Chemical Properties

• Appearance: /
• Storage Temp.: 2-8°C
• CAS DataBase Reference: N-Benzyloxycarbonyl-3-(4-chlorophenyl)-L-alanine(CAS DataBase Reference)
• NIST Chemistry Reference: N-Benzyloxycarbonyl-3-(4-chlorophenyl)-L-alanine(127888-10-2)
• EPA Substance Registry System: N-Benzyloxycarbonyl-3-(4-chlorophenyl)-L-alanine(127888-10-2)

Safety Data

• Hazardous Substances Data: 127888-10-2(Hazardous Substances Data)

Usage

General Description

N-Benzyloxycarbonyl-3-(4-chlorophenyl)-L-alanine is a chemical compound consisting of a benzyloxycarbonyl (Cbz) protecting group attached to an L-alanine molecule with a 4-chlorophenyl substitution. N-Benzyloxycarbonyl-3-(4-chlorophenyl)-L-alanine is commonly used in organic synthesis and as a building block for the preparation of peptides and other complex molecules. It is also a useful intermediate for the synthesis of pharmaceuticals and other biologically active compounds. The presence of the Cbz protecting group allows for selective manipulation of the amino acid during synthesis, making it a valuable tool for chemical research and drug development.

Upstream product

• 13139-17-8 N-(Benzyloxycarbonyloxy)succinimide 
• 134306-44-8 Z-DL-Phe(4Cl)OMe 
• 7424-00-2 DL-Phe(4Cl) 
• 394210-37-8 4-(4-chloro-benzyl)-2,5-dioxo-oxazolidine-3-carboxylic acid benzyl ester 
• 14173-39-8 p-chlorophenylalanine 
• 501-53-1 benzyl chloroformate 
• 127862-82-2 Z-DL-Phe(4Cl)-OCH₂CF₃ 

Downstream Products

• 14173-39-8 p-chlorophenylalanine 
• 1438257-70-5 cyclo(L-Am₇(SAc)-Aib-L-Phe(p-Cl)-D-Pro) 
• 1438257-67-0 C₂₅H₃₄BrClN₄O₄ 
• 609367-16-0 (R)-2-[(Benzyloxy-formyl-amino)-methyl]-hexanoic acid [(S)-2-(4-chloro-phenyl)-1-dimethylcarbamoyl-ethyl]-amide 
• 609367-48-8 2-amino-3-(4-chloro-phenyl)-N,N-dimethyl-propionamide 
• 609367-34-2 [(S)-2-(4-Chloro-phenyl)-1-dimethylcarbamoyl-ethyl]-carbamic acid benzyl ester 

Relevant articles and documents

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.

α-chymotrypsin-catalysed peptide synthesis via the kinetically controlled approach using activated esters as acyl donors in organic solvents with low water content: Incorporation of non-protein amino acids into peptides

The α-chymotrypsin-catalyzed peptide synthesis via the kinetically controlled approach using activated esters as acyl donors in orgnanic solvents with low water content was presented. The methyl esters of N-Z derivatives of racemic non-protein amino acids were chosen as carboxy components. They allowed the peptide-bond formation and optical resolution simultaneously to yield homochiral peptides. This method is useful for the incorporation of non-protein amino acids into peptides.