136814-99-8

Basic information

• Product Name: N-ACETYL-2-(4-FLUORO-PHENYL)-D-GLYCINE
• Synonyms: N-ACETYL-2-(4-FLUORO-PHENYL)-D-GLYCINE ;(R)-Acetylamino-(4-fluoro-phenyl)-acetic acid;(R)-2-acetaMido-2-(4-fluorophenyl)acetic acid;N-Ac-R-4-Fluorophenylglycine
• CAS NO: 136814-99-8
• Molecular Formula: C₁₀H₁₀FNO₃
• Molecular Weight: 211.1897032
• Mol File: 136814-99-8.mol

Chemical Properties

• Boiling Point: 439.2°C at 760 mmHg
• Flash Point: 219.4°C
• Appearance: /
• Density: 1.313g/cm³
• Vapor Pressure: 1.72E-08mmHg at 25°C
• Refractive Index: 1.537
• PKA: 3.14±0.10(Predicted)
• CAS DataBase Reference: N-ACETYL-2-(4-FLUORO-PHENYL)-D-GLYCINE(CAS DataBase Reference)
• NIST Chemistry Reference: N-ACETYL-2-(4-FLUORO-PHENYL)-D-GLYCINE(136814-99-8)
• EPA Substance Registry System: N-ACETYL-2-(4-FLUORO-PHENYL)-D-GLYCINE(136814-99-8)

Safety Data

• Hazardous Substances Data: 136814-99-8(Hazardous Substances Data)

Usage

Uses

Used in Pharmaceutical Industry:
N-ACETYL-2-(4-FLUORO-PHENYL)-D-GLYCINE is used as a pharmaceutical intermediate for the synthesis of various drugs, leveraging its structural components to create novel therapeutic agents.
Used in Medicinal Chemistry and Drug Discovery:
N-ACETYL-2-(4-FLUORO-PHENYL)-D-GLYCINE is utilized as a building block in the development of new drug candidates, enhancing their therapeutic properties and contributing to the advancement of medicinal chemistry.
Used in Pain Management:
N-ACETYL-2-(4-FLUORO-PHENYL)-D-GLYCINE is employed as an analgesic agent, providing pain relief through its inherent properties, which are beneficial in the management of various types of pain.
Used in Treatment of Inflammatory Disorders:
N-ACETYL-2-(4-FLUORO-PHENYL)-D-GLYCINE is used as an anti-inflammatory agent, modulating biological targets and biochemical pathways to alleviate inflammation and associated symptoms in various disorders.

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-/m1/s1

Upstream product

• 153381-37-4 N-acetyl-4-fluorophenylglycine 
• 60-35-5 acetamide 
• 201230-82-2 carbon monoxide 
• 459-57-4 4-fluorobenzaldehyde 
• 797039-94-2 N-(cyano(4-fluorophenyl)methyl)acetamide 
• 7292-73-1 (2RS)-N-(p-fluorophenyl)glycine 
• 56464-70-1 2-amino-2-(4-fluorophenyl)acetonitrile 

Relevant articles and documents

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.

HOMOCHIRAL HETEROORGANIC ANALOGS OF NATURAL COMPOUNDS. I. PREPARATIVE BIOCATALYTIC METHOD OF OBTAINING FLUORINE-CONTAINING L- AND D-PHENYLGLYCINES

A biocatalytic method of obtaining homochiral o- and p-fluorine-substituted phenylglycines by enantiomeric hydrolysis from N-phenylacetyl or N-acetyl derivatives under the action of Escherichia coli penicillin acylase or Streptoverticillium olivoreticuli aminoacylase is proposed.The L form of the amino acid and the unhydrolyzed D-enantiomer of the initial derivative are separated by extraction and chromatographic methods.The acid hydrolysis of the D-enantiomers of N-phenylacetyl derivatives of fluorine-substituted phenylglycines leads to partial (about 15percent) racemization.With a substantially higher (by two orders of magnitude) concentration of enzyme and an increase in the reaction time it is possible to use penicillinase as a catalyst for the hydrolysis of the D-enantiomer of the N-phenylacetyl derivative not accompanied by any appreciable racemization whatever.