401-28-5

Usage

Uses

Used in Pharmaceutical Industry:
Cbz-2-Fluoro-D-Phenylalanine is used as a building block for the synthesis of various pharmaceuticals and bioactive molecules. Its unique structure and properties allow for the development of new drugs and compounds with potential therapeutic applications.
Used in Medicinal Chemistry:
In the field of medicinal chemistry, Cbz-2-Fluoro-D-Phenylalanine serves as a key component in the design and synthesis of novel drug candidates. Its incorporation into molecular structures can enhance the pharmacological properties, such as potency, selectivity, and bioavailability, leading to the discovery of more effective treatments for various diseases and conditions.
Used in Organic Synthesis:
Cbz-2-Fluoro-D-Phenylalanine is also utilized in organic synthesis as a versatile intermediate for the preparation of a wide range of chemical compounds. Its reactivity and functional group compatibility make it a useful building block for the synthesis of complex organic molecules with diverse applications in various industries.

Upstream product

• 2629-55-2 2-fluoro-DL-phenylalanine 
• 501-53-1 benzyl chloroformate 
• 10466-61-2 (2S)-amino-4-methylpentanamide hydrochloride 
• 127862-79-7 Z-DL-Phe(2F)-OCH₂CF₃ 
• 127090-61-3 Z-DL-Phe(2F)OMe 
• 33208-99-0 (S)-alaninamide hydrochloride 

Downstream Products

• 126689-33-6 [1-[N',N'-Bis-(2-chloro-ethyl)-hydrazinocarbonyl]-2-(2-fluoro-phenyl)-ethyl]-carbamic acid benzyl ester 
• 127090-61-3 Z-DL-Phe(2F)OMe 
• 127862-79-7 Z-DL-Phe(2F)-OCH₂CF₃ 
• 126689-34-7 2-Amino-3-(2-fluoro-phenyl)-propionic acid N',N'-bis-(2-chloro-ethyl)-hydrazide; hydrobromide 
• 81727-43-7 diethyl N-(o-fluorophenyl-DL-alanyl)-1-aminoethylphosphonate 

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.

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.

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.