1100357-99-0

Basic information

• Product Name: Cbz-4-Bromo-D-Phenylalanine
• Synonyms: Cbz-4-Bromo-D-Phenylalanine;Cbz-D-4-Br-Phe-OH
• CAS NO: 1100357-99-0
• Molecular Formula: C17H16BrNO4
• Molecular Weight: 378.21724
• Mol File: 1100357-99-0.mol
• Article Data: 5

Chemical Properties

• Appearance: /
• CAS DataBase Reference: Cbz-4-Bromo-D-Phenylalanine(CAS DataBase Reference)
• NIST Chemistry Reference: Cbz-4-Bromo-D-Phenylalanine(1100357-99-0)
• EPA Substance Registry System: Cbz-4-Bromo-D-Phenylalanine(1100357-99-0)

Safety Data

• Hazardous Substances Data: 1100357-99-0(Hazardous Substances Data)

Upstream product

• 10466-61-2 (2S)-amino-4-methylpentanamide hydrochloride 
• 141971-13-3 Z-DL-Phe(4Br)OMe 
• 187028-22-4 Z-DL-Phe(4Br)-OCH₂CF₃ 
• 14091-15-7 p-bromo-DL-phenylalanine 
• 394210-38-9 4-(4-bromo-benzyl)-2,5-dioxo-oxazolidine-3-carboxylic acid benzyl ester 
• 24250-84-8 H-p-BrPhe-OH 
• 501-53-1 benzyl chloroformate 

Relevant articles and documents

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.

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.