136815-01-5

Usage

Uses

Used in Pharmaceutical Industry:
N-ACETYL-2-(4-FLUOROPHENYL)-L-GLYCINE is used as a pharmaceutical intermediate for the development of drugs targeting specific receptors or enzymes, due to its unique structural features that can be tailored for specific interactions with biological targets.
Used in Research and Development:
In the field of chemical research and development, N-ACETYL-2-(4-FLUOROPHENYL)-L-GLYCINE serves as a key component in the synthesis of new chemical entities, contributing to the discovery of novel therapeutic agents and diagnostic tools.
It is crucial to handle and store N-ACETYL-2-(4-FLUOROPHENYL)-L-GLYCINE according to safety guidelines to mitigate any potential health and environmental hazards associated with its use.

InChI:InChI=1/C10H10FNO3/c1-6(13)12-9(10(14)15)7-2-4-8(11)5-3-7/h2-5,9H,1H3,(H,12,13)(H,14,15)/t9-/m0/s1

Upstream product

• 60-35-5 acetamide 
• 201230-82-2 carbon monoxide 
• 459-57-4 4-fluorobenzaldehyde 
• 56464-70-1 2-amino-2-(4-fluorophenyl)acetonitrile 
• 797039-94-2 N-(cyano(4-fluorophenyl)methyl)acetamide 

Relevant academic research and scientific papers

Chemoenzymatic approaches to the dynamic kinetic asymmetric synthesis of aromatic amino acids

Enzymatic approaches for the production of amino acids by nitrilases are described. Dynamic kinetic asymmetric synthesis conditions were established for the aromatic aminonitriles, phenylglycinonitrile and 4- fluorophenylglycinonitrile, at high pH to produce the corresponding amino acid products in high enantiomeric excess. N-Acylation of aromatic aminonitriles led to spontaneous racemization at pH 8, allowing preferential enzymatic hydrolysis of the (R)-enantiomer to afford the product N-acylamino acids in up to 99% enantiomeric excess (ee).

Efficient chemoenzymatic synthesis of enantiomerically pure α-amino acids

A general two-step chemoenzymatic synthesis for enantiomerically pure natural and nonnatural α-amino acids is presented. In the first step of the sequence, the ubiquitous educts aldehyde, amide and carbon monoxide react by palladium-catalyzed amidocarbonylation to afford the racemic N-acyl amino acids in excellent yields. In the second step, enzymatic enantioselective hydrolysis yields the free optically pure a-amino acid and the other enantiomer as the N-acyl derivative, both in optical purities of 85-99.5% ee. The advantage of the chemoenzymatic process compared to other amino acid synthesis are demonstrated by the preparation of various functionalized (-OR, -Cl, -F, -SR) α-amino acids on a 10-g scale.