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Usage

Uses

Used in Pharmaceutical Research:
Cbz-L-Phe(3-Cl)-OH is utilized as a key building block in the synthesis of pharmaceutical compounds, contributing to the development of new drugs and therapeutic agents. Its unique structure allows for the creation of a variety of bioactive molecules with potential medicinal properties.
Used in Organic Synthesis:
In the field of organic synthesis, Cbz-L-Phe(3-Cl)-OH serves as a versatile intermediate, enabling the construction of complex organic molecules. Its reactivity and functional groups facilitate multiple synthetic pathways, making it a valuable component in the preparation of a range of organic compounds.
Used in Chemical Education and Research:
Cbz-L-Phe(3-Cl)-OH is also employed as an educational tool in chemistry, providing students and researchers with a practical example of an amino acid derivative and its applications in chemical reactions. It aids in understanding the principles of organic chemistry and the synthesis of pharmaceutically relevant compounds.
Used in Chemical Manufacturing Industry:
Cbz-L-Phe(3-Cl)-OH is used as a raw material in the production of various chemical products, particularly those related to the pharmaceutical and healthcare sectors. Its presence in the manufacturing process underscores its importance in the synthesis of a wide array of chemical entities with diverse applications.

Upstream product

• 1956-15-6 3-chlorophenylalanine 
• 501-53-1 benzyl chloroformate 
• 10466-61-2 (2S)-amino-4-methylpentanamide hydrochloride 
• 80126-51-8 (2S)-2-amino-3-(3-chlorophenyl)propanoic acid 

Relevant academic research and scientific papers

Discovery of Fluoromethylketone-Based Peptidomimetics as Covalent ATG4B (Autophagin-1) Inhibitors

ATG4B or autophagin-1 is a cysteine protease that cleaves ATG8 family proteins. ATG4B plays essential roles in the autophagosome formation and the autophagy pathway. Herein we disclose the design and structural modifications of a series of fluoromethylketone (FMK)-based peptidomimetics as highly potent ATG4B inhibitors. Their structure-activity relationship (SAR) and protease selectivity are also discussed.

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.