55478-54-1

Basic information

• Product Name: Z-DL-PHE(4-CL)-OH
• Synonyms: N-ALPHA-CARBOBENZOXY-DL-(4-CHLORO)PHENYLALANINE;Z-P-CHLORO-DL-PHE-OH;Z-DL-PHE(4-CI)-OH;Z-DL-PHE(4-CL)-OH;Z-4-CHLORO-DL-PHENYLALANINE;CBZ-DL-4-CHLOROPHENYLALANINE;4-Chloro-N-[(phenylmethoxy)carbonyl]-DL-phenylalanine;(RS)-Z-2-amino-3-(4-chlorophenyl)propionic acid
• CAS NO: 55478-54-1
• Molecular Formula: C₁₇H₁₆ClNO₄
• Molecular Weight: 333.77
• Mol File: 55478-54-1.mol

Chemical Properties

• Appearance: /
• Storage Temp.: Store at 0-5°C
• CAS DataBase Reference: Z-DL-PHE(4-CL)-OH(CAS DataBase Reference)
• NIST Chemistry Reference: Z-DL-PHE(4-CL)-OH(55478-54-1)
• EPA Substance Registry System: Z-DL-PHE(4-CL)-OH(55478-54-1)

Safety Data

• Hazardous Substances Data: 55478-54-1(Hazardous Substances Data)

Usage

Chemical Properties

White powder

Upstream product

• 127862-82-2 Z-DL-Phe(4Cl)-OCH₂CF₃ 
• 10466-61-2 (2S)-amino-4-methylpentanamide hydrochloride 
• 7424-00-2 DL-Phe(4Cl) 
• 501-53-1 benzyl chloroformate 
• 134306-44-8 Z-DL-Phe(4Cl)OMe 

Downstream Products

• 78835-68-4 {1-[2-Amino-3-(4-chloro-phenyl)-propionylamino]-ethyl}-phosphonic acid 
• 127862-82-2 Z-DL-Phe(4Cl)-OCH₂CF₃ 
• 134306-44-8 Z-DL-Phe(4Cl)OMe 
• 78835-67-3 {1-[2-Benzyloxycarbonylamino-3-(4-chloro-phenyl)-propionylamino]-ethyl}-phosphonic acid diethyl ester 

Relevant articles and documents

Superiority of the carbamoylmethyl ester as an acyl donor for the kinetically controlled amide-bond formation mediated by α-chymotrypsin

The superiority of the carbamoylmethyl ester as an acyl donor for the α-chymotrypsin-catalysed kinetically controlled peptide-bond formation is demonstrated in the couplings of an inherently poor amino acid substrate, Ala, with various amino acid residues as amino components and in the couplings of non-protein amino acids such as halogenophenylalanines as carboxylic components. Furthermore, this approach is applied to the amide-bond formation between an amino acid residue and a chiral amine, which is highly diastereoselective.

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.

α-Chymotrypsin-catalysed peptide synthesis using activated esters as acyl donors

The coupling efficiency in α-chymotrypsin-catalysed peptide synthesis is greatly improved by the use of activated esters such as the 2,2,2-trifluoroethyl ester as acyl donor instead of the conventional methyl ester; this approach is useful for the incorporation of non-protein amino acids into peptides.

3,5-substituted 4,5-dihydroisoxazoles as transglutaminase inhibitors

The present invention is directed to certain 3,5 substituted, 4,5-dihydroisoxazoles, and methods for their use. These compounds are transgulatminase inhibitors, and are particularly effective in the inhibition of epidermal transglutaminase and the treatment of acne.

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.