123098-44-2

Usage

Uses

Used in Pharmaceutical Industry:
Cbz-2-Bromo-D-Phenylalanine is used as a building block for the synthesis of peptide-based drugs and therapeutic agents, contributing to the development of novel compounds with potential biological activity.
Used in Organic Synthesis:
Cbz-2-Bromo-D-Phenylalanine is used as a versatile substrate for the modification of natural amino acids, enabling the creation of new compounds with potential applications in various fields.
Used in Peptide Chemistry:
Cbz-2-Bromo-D-Phenylalanine is utilized in the synthesis of peptides, providing a foundation for the development of peptide libraries for drug discovery and development applications.
Used in Chemical Research:
Due to its unique structure and reactivity, Cbz-2-Bromo-D-Phenylalanine serves as a valuable tool for chemical research, aiding in the exploration of new synthetic pathways and the understanding of molecular interactions.

Upstream product

• 10466-61-2 (2S)-amino-4-methylpentanamide hydrochloride 
• 423763-16-0 Z-(RS)-Phe(2Br)-ON=C(CH₃)2 
• 203640-55-5 Z-(RS)-Phe(2Br)-OCH₂CF₃ 
• 203640-56-6 z-(RS)-Phe(2Br)-O-carbamoylmethyl 
• 1991-79-3 2-amino-3-(2-bromophenyl)propanoic acid 
• 501-53-1 benzyl chloroformate 

Downstream Products

• 256474-48-3 Z-(RS)-Phe(2Br)-OMe 
• 203640-55-5 Z-(RS)-Phe(2Br)-OCH₂CF₃ 
• 423763-14-8 Z-(RS)-Phe(2Br)-OCH₂CH₂Cl 
• 423763-13-7 Z-(RS)-Phe(2Br)-OCH₂CF₂CF₃ 

Relevant academic research and scientific papers

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.

Remarkable effects of donor esters on the α-chymotrypsin-catalyzed couplings of inherently poor amino acid substrates

The extremely low efficiency during the α-chymotrypsin-catalyzed coupling of an inherently poor amino acid substrate, e.g., alanine, using the methyl ester as an acyl donor was significantly improved using esters such as the 2,2,2-trifluoroethyl or carbamoylmethyl ester. The ameliorating effect of the latter ester was especially significant.