49759-64-0

Usage

Uses

Used in Peptide Synthesis:
CBZ-L-3-Fluorophenylalanine is utilized as a building block in peptide synthesis, allowing for the creation of modified peptides with tailored properties or functions. Its incorporation into peptides can lead to altered biological activities, making it a key component in the development of novel therapeutic agents.
Used in Pharmaceutical Development:
In the pharmaceutical industry, CBZ-L-3-Fluorophenylalanine is employed as a precursor in the synthesis of potential drug candidates. Its effects on protein structure and function make it a valuable tool in the design of new medications, particularly those targeting specific biological pathways or mechanisms.
Used in Drug Design:
CBZ-L-3-Fluorophenylalanine is used in drug design to explore its potential as a therapeutic agent. Its unique chemical properties and ability to modify peptide behavior offer opportunities for developing innovative treatments for various diseases and conditions.
Used in Biochemical Research:
In the field of biochemistry, CBZ-L-3-Fluorophenylalanine serves as a research tool to study the effects of amino acid modifications on protein structure, function, and interactions. This knowledge can contribute to a deeper understanding of biological processes and the development of targeted therapies.
Overall, CBZ-L-3-Fluorophenylalanine's diverse applications across various industries highlight its significance in advancing scientific knowledge and fostering the creation of new therapeutic solutions.

Upstream product

• 19883-77-3 L-3-fluorophenylalanine 
• 501-53-1 benzyl chloroformate 
• 127862-80-0 Z-DL-Phe(3F)-OCH₂CF₃ 
• 456-41-7 1-(Bromomethyl)-3-fluorobenzene 
• 49759-51-5 2-Benzyloxycarbonylamino-2-(3-fluoro-benzyl)-malonic acid dimethyl ester 
• 49864-42-8 2-Benzyloxycarbonylamino-2-(3-fluoro-benzyl)-malonic acid monomethyl ester 
• 49759-56-0 Z-DL-Phe(3F)-OMe 
• 37447-35-1 2-benzyloxycarbonylaminomalonic acid dimethyl ester 

Downstream Products

• 87184-30-3 Cbz-L-m-FPhe-L-Ala-OBzl 
• 19883-77-3 L-3-fluorophenylalanine 
• 205493-82-9 (3S,4S)-3-{N-benzyloxycarbonyl-β-(3-fluorophenyl)-L-alanyl}-amino-4-acetoxy-azetidin-2-one 
• 87184-16-5 L-m-FPhe-L-Ala-L-Ala 
• 87184-20-1 L-m-FPhe-L-Ala 
• 87184-27-8 Cbz-L-m-FPhe-L-Ala-L-Ala-OBzl 

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.

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.

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.