18125-46-7

Basic information

• Product Name: 4-Fluoro-D-phenylalanine
• Synonyms: D-4-FLUOROPHE;D-4-FLUOROPHENYLALANINE;H-D-PHE(P-F)-OH;H-D-PHE(4-F)-OH;H-P-FLUORO-D-PHE-OH;4-FLUORO-D-PHENYLALANINE;P-FLUORO-D-PHENYLALANINE;(R)-2-AMINO-3-(4-FLUORO-PHENYL)-PROPIONIC ACID
• CAS NO: 18125-46-7
• Molecular Formula: C₉H₁₀FNO₂
• Molecular Weight: 183.18
• Product Categories: Amino Acids;Phenylalanine analogs and other aromatic alpha amino acids;Peptide;a-amino
• Mol File: 18125-46-7.mol
• Article Data: 27

Chemical Properties

• Melting Point: ~245 °C (dec.)
• Boiling Point: 313.3ºCat760mmHg
• Flash Point: 143.3ºC
• Appearance: /
• Density: 1.1939 (estimate)
• Storage Temp.: Store at RT.
• PKA: 2.20±0.10(Predicted)
• BRN: 2416149
• CAS DataBase Reference: 4-Fluoro-D-phenylalanine(CAS DataBase Reference)
• NIST Chemistry Reference: 4-Fluoro-D-phenylalanine(18125-46-7)
• EPA Substance Registry System: 4-Fluoro-D-phenylalanine(18125-46-7)

Safety Data

• Hazard Codes: Harmful:
• Safety Statements: 22-24/25
• WGK Germany: 3
• Hazardous Substances Data: 18125-46-7(Hazardous Substances Data)

Usage

Description

4-Fluoro-D-Phenylalanine is an amino acid derivative characterized by the presence of a fluorine atom at the 4th position of the phenyl ring in its D-configuration. It is a white to off-white powder and is known for its unique chemical properties that make it a valuable compound in various applications.

Uses

Used in Pharmaceutical Industry:
4-Fluoro-D-Phenylalanine is used as a building block for the preparation of new peptidomimetics. Its unique chemical properties allow for the development of novel compounds with potential therapeutic applications, particularly in the area of drug design and development.
Used in Research and Development:
In the field of research and development, 4-Fluoro-D-Phenylalanine serves as an important compound for studying the effects of fluorination on the properties and functions of amino acids. This knowledge can be applied to the design of new drugs and the understanding of protein structures and interactions.
Used in Chemical Synthesis:
4-Fluoro-D-Phenylalanine is also utilized in chemical synthesis, where its fluorinated structure can be exploited to create a variety of new compounds with different properties and potential applications in various industries, such as pharmaceuticals, agrochemicals, and materials science.

Upstream product

• 69216-82-6 (R)-N-acetyl-p-fluorophenylalanine 
• 1994-30-5 Sodium; 3-(4-fluoro-phenyl)-2-oxo-propionate 
• 135950-34-4 3-(4-Fluoro-phenyl)-2-{[1-phenyl-meth-(E)-ylidene]-amino}-propionic acid ethyl ester 
• 654054-42-9 (R)-2-Amino-1-((1S,5R,7R)-10,10-dimethyl-3,3-dioxo-3λ⁶-thia-4-aza-tricyclo[5.2.1.0^1,5]dec-4-yl)-3-(4-fluoro-phenyl)-propan-1-one 
• 7761-30-0 sodium 3-(4-fluorophenyl)-2-oxopropionate 
• 404-32-0 DL-Z-4-F-Phe-OH 
• 654054-26-9 ((1S,5R,7R)-10,10-Dimethyl-3,3-dioxo-3λ⁶-thia-4-aza-tricyclo[5.2.1.0^1,5]dec-4-yl)-[(2R,3R)-3-(4-fluoro-phenyl)-aziridin-2-yl]-methanone 
• 459-46-1 4-Fluorobenzyl bromide 
• 51-65-0 4-Fluorophenylalanine 
• 110728-27-3 (R,S)-N-phenylacetyl-4-fluorophenylalanine 
• 380-71-2 diethyl α-acetamido, α-(4-fluorobenzyl)malonate 
• 17481-06-0 rac-Ac-p-F-Phe-OH 
• 103-81-1 Benzeneacetamide 
• 64282-12-8 4-fluoro-DL-phenylalanine methyl ester hydrochloride 

Downstream Products

• 117467-73-9 (R)-(N-benzyloxycarbonyl)-p-fluorophenylalanine 
• 200267-65-8 (R)-2-Amino-3-(4-fluorophenyl)-1-propanol 
• 124980-94-5 (2R)-3-(4-fluorophenyl)-2-hydroxypropanoic acid 
• 1300006-84-1 (R)-N-[(S)-1-[(6-amino-pyridin-3-ylmethyl)-carbamoyl]-2-(3,4-difluoro-phenyl)-ethyl]-3-(4-fluoro-phenyl)-2-hydroxy-propionamide trifluoroacetate 
• 874336-38-6 C₂₅H₃₁FN₂O₅ 
• 874440-04-7 C₂₀H₂₃FN₂O₃ 
• 1351469-20-9 C₄₃H₅₅FN₄O₇ 
• 1351469-21-0 C₃₁H₄₁FN₄O₅ 
• 203732-76-7 C₁₆H₁₆FNO₂ 
• 874336-40-0 C₅₀H₆₁FN₄O₉ 
• 1351469-17-4 C₄₂H₅₅FN₄O₇ 
• 874336-42-2 (R)-2-((R)-2-((S)-2-(((R)-2-(2-(3-aminopropyl)phenoxy)propyl)-amino)-2-cyclopropyl-N-methylacetamido)propanamido)-3-(4-fluorophenyl)propanoic acid 
• 874336-39-7 C₂₀H₂₃FN₂O₃*ClH 
• 874336-43-3 C₃₀H₃₉FN₄O₄*ClH 

Relevant articles and documents

A novel phenylalanine ammonia-lyase from Pseudozyma antarctica for stereoselective biotransformations of unnatural amino acids

A novel phenylalanine ammonia-lyase of the psychrophilic yeast Pseudozyma antarctica (PzaPAL) was identified by screening microbial genomes against known PAL sequences. PzaPAL has a significantly different substrate binding pocket with an extended loop (26 aa long) connected to the aromatic ring binding region of the active site as compared to the known PALs from eukaryotes. The general properties of recombinant PzaPAL expressed in E. coli were characterized including kinetic features of this novel PAL with L-phenylalanine (S)-1a and further racemic substituted phenylalanines rac-1b-g,k. In most cases, PzaPAL revealed significantly higher turnover numbers than the PAL from Petroselinum crispum (PcPAL). Finally, the biocatalytic performance of PzaPAL and PcPAL was compared in the kinetic resolutions of racemic phenylalanine derivatives (rac-1a-s) by enzymatic ammonia elimination and also in the enantiotope selective ammonia addition reactions to cinnamic acid derivatives (2a-s). The enantiotope selectivity of PzaPAL with o-, m-, p-fluoro-, o-, p-chloro- and o-, m-bromo-substituted cinnamic acids proved to be higher than that of PcPAL.

Deracemization and stereoinversion to aromatic d-amino acid derivatives with ancestral l-amino acid oxidase

Enantiomerically pure amino acid derivatives could be foundational compounds for peptide drugs. Deracemization of racemates to l-amino acid derivatives can be achieved through the reaction of evolved d-amino acid oxidase and chemical reductants, whereas deracemization to d-amino acid derivatives has not progressed due to the difficulty associated with the heterologous expression of l-amino acid oxidase (LAAO). In this study, we succeeded in developing an ancestral LAAO (AncLAAO) bearing broad substrate selectivity (13 l-amino acids) and high productivity through an Escherichia coli expression system (50.7 mg/L). AncLAAO can be applied to perform deracemization to d-amino acids in a similar way to deracemization to l-amino acids. In fact, full conversion (>99% ee, d-form) could be achieved for 16 racemates, including nine d,l-Phe derivatives, six d,l-Trp derivatives, and a d,l-phenylglycine. Taken together, we believe that AncLAAO could be a key enzyme to obtain optically pure d-amino acid derivatives in the future.

One-Pot Enzymatic Synthesis of d-Arylalanines Using Phenylalanine Ammonia Lyase and l-Amino Acid Deaminase

The phenylalanine ammonia-lyase (AvPAL) from Anabaena variabilis catalyzes the amination of substituent trans-cinnamic acid (t-CA) to produce racemic d,l-enantiomer arylalanine mixture owing to its low stereoselectivity. To produce high optically pure d-arylalanine, a modified AvPAL with high d-selectivity is expected. Based on the analyses of catalytic mechanism and structure, the Asn347 residue in the active site was proposed to control stereoselectivity. Therefore, Asn347 was mutated to construct mutant AvPAL-N347A, the stereoselectivity of AvPAL-N347A for d-enantiomer arylalanine was 2.3-fold higher than that of wild-type AvPAL (WtPAL). Furthermore, the residual l-enantiomer product in reaction solution could be converted into the d-enantiomer product through stereoselective oxidation by PmLAAD and nonselective reduction by reducing agent NH3BH3. At optimal conditions, the conversion rate of t-CA and optical purity (enantiomeric excess (eeD)) of d-phenylalanine reached 82% and exceeded 99%, respectively. The two enzymes displayed activity toward a broad range of substrate and could be used to efficiently synthesize d-arylalanine with different groups on the phenyl ring. Among these d-arylalanines, the yield of m-nitro-d-phenylalanine was highest and reached 96%, and the eeD exceeded 99%. This one-pot synthesis using AvPAL and PmLAAD has prospects for industrial application.