1132-68-9

Basic information

• Product Name: L-4-Fluorophenylalanine
• Synonyms: (S)-2-AMINO-3-(4-FLUORO-PHENYL)-PROPIONIC ACID;RARECHEM BK PT 0031;P-FLUORO-L-PHENYLALANINE;P-FLUORO-PHENYLALANINE;H-L-PHE(4-F)-OH;H-PHE(4-F)-OH;H-PHE(P-F)-OH;H-P-FLUORO-PHE-OH
• CAS NO: 1132-68-9
• Molecular Formula: C₉H₁₀FNO₂
• Molecular Weight: 183.18
• EINECS: 145-896-5
• Product Categories: Amino Acids;Phenylalanine analogs and other aromatic alpha amino acids;Phenylalanine [Phe, F];Unusual Amino Acids;Amino hydrochloride;a-amino;Non-natural amino acids
• Mol File: 1132-68-9.mol

Chemical Properties

• Melting Point: ~255 °C (dec.)
• Boiling Point: 313.3 °C at 760 mmHg
• Flash Point: 143.3 °C
• Appearance: white to off-white powder
• Density: 1.1939 (estimate)
• Vapor Pressure: 2.64E-05mmHg at 25°C
• Storage Temp.: Store at RT.
• PKA: 2.20±0.10(Predicted)
• Water Solubility: Soluble in water and 0.5M HCl (50 mg/ml).
• BRN: 2416148
• CAS DataBase Reference: L-4-Fluorophenylalanine(CAS DataBase Reference)
• NIST Chemistry Reference: L-4-Fluorophenylalanine(1132-68-9)
• EPA Substance Registry System: L-4-Fluorophenylalanine(1132-68-9)

Safety Data

• Safety Statements: 23-24/25
• WGK Germany: 3
• RTECS: DW1765000
• Hazardous Substances Data: 1132-68-9(Hazardous Substances Data)

Usage

Uses

Used in Pharmaceutical Research:
L-4-Fluorophenylalanine is used as a pharmaceutical research compound for studying the regulation of tyrosine hydroxylase, an enzyme involved in the synthesis of neurotransmitters such as dopamine and norepinephrine. This research can help in understanding the mechanisms of various neurological disorders and developing potential therapeutic agents.
Used in Biochemical Studies:
L-4-Fluorophenylalanine is used as a biochemical research tool to investigate the structure and function of enzymes and proteins that interact with L-phenylalanine. Its unique fluoro substitution allows researchers to probe the active sites of enzymes and study the effects of this modification on enzyme activity and specificity.
Used in Drug Development:
L-4-Fluorophenylalanine can be used in drug development as a building block for the synthesis of novel compounds with potential therapeutic applications. Its unique chemical properties may provide advantages in terms of selectivity, potency, and pharmacokinetics compared to other analogs.
Used in Chemical Synthesis:
L-4-Fluorophenylalanine can be used as a starting material or intermediate in the synthesis of various organic compounds, including pharmaceuticals, agrochemicals, and other specialty chemicals. Its fluoro substitution may impart unique reactivity or selectivity in chemical reactions, enabling the development of new synthetic routes and products.

Purification Methods

It is recrystallised from aqueous EtOH. The (R)-N-acetyl derivative has m 142-145o, [] D -38.6o (c 8, EtOH). [Bennett & Nieman J Am Chem Soc 72 1800 1950, Beilstein 14 III 1268.]

InChI:InChI:1S/C9H10FNO2/c10-7-3-1-6(2-4-7)5-8(11)9(12)13/h1-4,8H,5,11H2,(H,12,13)

Upstream product

• 453-82-7 N-acetyl-3-fluoro-L-phenylalanine-(N'-phenyl-hydrazide) 
• 7761-30-0 sodium 3-(4-fluorophenyl)-2-oxopropionate 
• 39801-54-2 N-(trifluoroacetyl)-p-fluoro-DL-phenylalanine 
• 1994-30-5 Sodium; 3-(4-fluoro-phenyl)-2-oxo-propionate 
• 123052-79-9 tert-butyl (2S,5S)-2-(tert-butyl)-5-(4-fluorobenzyl)-3-methyl-4-oxo-1-imidazolidinecarboxylate 
• 113845-29-7 N-acetyl-S-phenylalanine S(-)-α-phenylethylamide 
• 56-40-6 glycine 
• 352-11-4 1-chloromethyl-4-fluorobenzene 
• 110728-27-3 (R,S)-N-phenylacetyl-4-fluorophenylalanine 
• 17543-58-7 2S-2-benzyloxycarbonylamino-2-(4-fluorophenylmethyl)-acetic acid 
• 73283-54-2 (S)-methyl 2-amino-3-(4-fluorophenyl)propanoate 
• 135950-34-4 3-(4-Fluoro-phenyl)-2-{[1-phenyl-meth-(E)-ylidene]-amino}-propionic acid ethyl ester 
• 17481-06-0 rac-Ac-p-F-Phe-OH 
• 330-81-4 (S)-2-acetylamino-3-(4-fluorophenyl)propionic acid 

Downstream Products

• 41153-30-4 Boc-Phe(p-F) 
• 2251-76-5 2-(4-fluorophenyl)-2-oxoacetic acid 
• 37562-60-0 N-trifluoroacetyl-L-4-fluorophenylalanine 
• 78818-27-6 o-nitrobenzenesulfenyl-p-fluorophenylalanine 
• 176896-72-3 (S)-methyl 2-amino-3-(4-fluorophenyl)propanoate hydrochloride 
• 167256-37-3 (S)-2-Acetylsulfanyl-3-(4-fluoro-phenyl)-propionic acid 
• 199340-82-4 (S)-3-(4-Fluoro-phenyl)-2-heptanoylamino-propionic acid 
• 330-81-4 (S)-2-acetylamino-3-(4-fluorophenyl)propionic acid 
• 17543-58-7 2S-2-benzyloxycarbonylamino-2-(4-fluorophenylmethyl)-acetic acid 
• 124980-97-8 (S)-methyl-2-hydroxy-3-(4-fluorophenyl)propionate 
• 124980-93-4 (S)-3-(4-fluorophenyl)-2-hydroxypropionic acid 
• 151911-23-8 (R)-β-amino-β-(4-fluorophenyl)propionic acid 
• 152485-69-3 (-)-1-(4-fluoro-phenyl)-2-propanol 
• 882149-30-6 (S)-3-(4-fluorophenyl)-1,2-propanediol 

Relevant articles and documents

Mechanism-inspired engineering of phenylalanine aminomutase for enhanced β-regioselective asymmetric amination of cinnamates

Turn to switch: A mutant of phenylalanine aminomutase was engineered that can catalyze the regioselective amination of cinnamate derivatives (see scheme, red) to, for example, β-amino acids. This regioselectivity, along with the X-ray crystal structures, suggests two distinct carboxylate binding modes differentiated by Cβi￡Cipso bond rotation, which determines if β- (see scheme) or α-addition takes place. Copyright

Bio-inspired enantioselective full transamination using readily available cyclodextrin

The mimics of vitamin B6-dependent enzymes that catalyzed an enantioselective full transamination in the pure aqueous phase have been realized for the first time through the establishment of a new “pyridoxal 5′-phosphate (PLP) catalyzed non-covalent cyclodextrin (CD)-keto acid inclusion complexes” system, and various optically active amino acids have been obtained.

THE INCLUSION OF THE ENANTIOMERS OF N-TRIFLUOROACETYL-4-FLUOROPHENYLALANINE AND N-TRIFLUOROACETYLPHENYLALANINE BY CYCLOMALTOHEXAOSE: A 2H- AND 19F-N.M.R. STUDY

19F-N.m.r. studies show that N-trifluoroacetyl-D- and -L-4-fluorophenylalanine and N-trifluoroacetyl-D- and -L-phenylalanine form 1:1 inclusion complexes with cyclomaltohexaose (α-cyclodextrin) characterised by stability constants of 11.44 +/- 1.13, 11.40 +/- 1.09, 6.15 +/- 0.59, and 6.37 +/- 0.81 M-1, respectively, in aqueous 0.1M NaCl at pH 6.5 and 25 deg C.Under similar conditions, the correlation time of N-trifluoroacetyl-phenylalanine changed from 65 +/- 4 ps in the free state to 320 +/- 40 ps in the complex, consistent with there being little freedom of movement of the guest in the inclusion complex.

Acylase I catalysed hydrolysis of para-substituted (S)-phenylalanine derivatives from mixtures of the racemic ortho- and para-substituted isomers

para-Substituted (S)-phenylalanines may be obtained by treatment of the corresponding mixtures of ortho- and para-substituted N-acetyl-(RS)- phenylalanines with Acylase I from porcine kidney. The selectivity of the enzyme may be attributed to its evolution to digest peptide derivatives of (S)-phenylalanine and (S)-tyrosine.

A new approach to the efficient method for the asymmetric synthesis of (S)-O-, M-, P-fluorophenylalanines and their 2-methyl-substituted analogs

The reactions of asymmetric C-alkylation of glycine and alanine in NiII complexes of their Schiff's bases with modified chiral auxiliaries (S)-2-N-[(N0-2-chlorobenzylprolyl)- amino]benzophenone and (S)-2-N-[N′-(3, 4-dimethylbenzylprolyl)amino]benzophenone by fluorine-substituted benzyl halogenides have been studied. As a result, a highly stereoselective and relatively rapid method for the asymmetric synthesis of (S)-o-, m-, p-fluorophenylalanines and their 2-methyl substituted analogs has been developed.

Asymmetric synthesis of organoelement analogues of natural products; Part 12: General method for the asymmetric synthesis of fluorine-containing phenylalanines and α-methyl(phenyl)alanines via alkylation of the chiral nickel(II) Schiff's base complexes of

Nickel(II) complexes of Schiff's bases derived from (S)-o-[(N-benzyl]prolyl)amino]benzophenone [N-(2-benzoylphenyl)-1-benzylpyrrolidine-2-carboxamide] (BBP) and glycine or alanine have been used for asymmetric synthesis of fluoro (S)-phenylalanines and (S

ASYMMETRIC SYNTHESIS OF HETEROORGANIC ANALOGS OF NATURAL COMPOUNDS. 2. A CONVENIENT PREPARATIVE METHOD FOR THE SYNTHESIS OF ENANTIOMERICALLY PURE (S)-(-)-o-, m-, and p-FLUOROPHENYLALANINES AND THEIR 2-METHYL-SUBSTITUTED ANALOGS.

A convenient preparative method for the synthesis of the enantiomerically pure o-, m-, and p-fluorophenylalanines and their α-methyl-substituted analogs by means of the alkylation with the corresponding fluorine-containing benzyl chlorides of glycine and

Biocatalytic stereoinversion of d-: Para -bromophenylalanine in a one-pot three-enzyme reaction

Halogenated derivatives of phenylalanine can be used as cross-coupling reagents for making drug-like molecules, and pure enantiomers of these precursors are therefore highly desirable. In our exploration of enzymatic routes to simplify the deracemisation process, the application of two enzymes, d-amino acid transaminase and phenylalanine dehydrogenase, both from Lysinibacillus sphaericus, has given promising results for the stereo-inversion of d-enantiomers of para-bromophenylalanine as the model substrate and also p-chloro/fluorophenylalanine and tyrosine. The addition of a coenzyme recycling system using ethanol and alcohol dehydrogenase reduced the amount of coenzyme needed for the reaction catalysed by phenylalanine dehydrogenase, reducing cost and permitting efficient and complete conversion of the racemic amino acids to the l-enantiomer. Relative proportions of the enzymes were optimized. The high purity of the l-enantiomer, with an ee over 99%, and the ease of the process make it an ideal alternative for deracemisation of the studied compounds.

Engineering of phenylalanine ammonia lyase from Rhodotorula graminis for the enhanced synthesis of unnatural L-amino acids

Phenylalanine ammonia lyase (PAL) catalyses the reversible non-oxidative deamination of phenylalanine to trans-cinnamic acid and ammonia. Analogues of L-phenylalanine are incorporated as pharmacophores in several peptidomimetic drug molecules and are therefore of particular interest to the fine chemical industry. PAL from Rhodotorula graminis (RgrPAL) has shown an ability to accept analogues of L-phenylalanine. Our aim was to increase enzymatic activity with directed evolution towards a specific non-natural substrate through the cloning and over-production of PAL in Escherichia coli. The identified variants of RgrPAL with significantly showed more catalytic efficient compared to the wild-type enzyme. These variants were used in a preparative scale biotransformation resulting in a 94% conversion to L-4-Br-phenylalanine (>99% ee).

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.