51-65-0

Usage

Uses

Used in Pharmaceutical Industry:
DL-3-(4-Fluorophenyl)alanine is used as an intermediate in the synthesis of various pharmaceutical compounds for [application reason]. Its unique structure allows for the development of new drugs with improved properties, such as enhanced bioavailability, selectivity, and potency.
Used in Chemical Synthesis:
DL-3-(4-Fluorophenyl)alanine is used as a building block in the chemical synthesis of various organic compounds for [application reason]. Its fluorinated structure can be exploited to create novel molecules with specific properties, such as increased stability or reactivity.
Used in Research and Development:
DL-3-(4-Fluorophenyl)alanine is used as a research tool for studying the effects of fluorination on the properties and functions of phenylalanine-containing molecules for [application reason]. This can provide valuable insights into the structure-activity relationships of these compounds and guide the design of new molecules with desired properties.
Used in Material Science:
DL-3-(4-Fluorophenyl)alanine is used in the development of new materials with specific properties, such as improved mechanical strength, thermal stability, or chemical resistance for [application reason]. Its unique structure can be incorporated into polymers or other materials to enhance their performance.

Air & Water Reactions

Insoluble in water.

Reactivity Profile

DL-3-(4-Fluorophenyl)alanine may be sensitive to exposure to light. A fluorinated amino acid. This is a neutral to slightly acidic material. DL-3-(4-Fluorophenyl)alanine may react as an organic amine or acid, although, its reactivity is moderated considerably by the presence of the other group.

Health Hazard

SYMPTOMS: DL-3-(4-Fluorophenyl)alanine is a phenylalanine antagonist and may cause inhibition of protein synthesis.

Fire Hazard

Flash point data for DL-3-(4-Fluorophenyl)alanine are not available; however, DL-3-(4-Fluorophenyl)alanine is probably combustible.

Biochem/physiol Actions

Inhibits mitosis and reversibly arrests HeLa cells in G2.

InChI:InChI=1/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

• 17481-06-0 rac-Ac-p-F-Phe-OH 
• 459-32-5 4-fluorocinnamic acid 
• 459-32-5 (E)-4-fluorocinnamic acid 
• 1132-68-9 L-4-fluorophenylalanine 
• 80980-62-7 (+/-)-15-aminomethyl-14-hydroxy-5,5-dimethyl-2,8-dithia<9>(2,5)pyridophane 
• 1994-30-5 Sodium; 3-(4-fluoro-phenyl)-2-oxo-propionate 
• 587-76-8 α-benzoylamino-4-fluoro-cinnamic acid 
• 138996-53-9 (Z)-ethyl 2-benzamido-3-(4-fluorophenyl)acrylate 
• 380-71-2 diethyl α-acetamido, α-(4-fluorobenzyl)malonate 
• 449-81-0 (4Z)-2-phenyl-4-[(4-fluorophenyl)methylidene]-1,3-oxazol-5(4H)-one 
• 1353886-54-0 ethyl 3-(4-fluorophenyl)-2-(hydroxyimino)propanoate 

Downstream Products

• 39801-54-2 N-(trifluoroacetyl)-p-fluoro-DL-phenylalanine 
• 153889-27-1 N-phthaloyl-DL-(4-fluorophenyl)alanine 
• 82283-58-7 (Z)-2-(2-Amino-acetylamino)-3-(4-fluoro-phenyl)-acrylic acid 
• 82283-52-1 (Z)-2-(2-Chloro-acetylamino)-3-(4-fluoro-phenyl)-acrylic acid 
• 41153-30-4 Boc-Phe(p-F) 
• 1114547-60-2 N-(3-chloro-4-cyanophenyl)-4-fluorophenylalanine 
• 211681-79-7 C₁₁H₁₂FNO₄ 
• 191930-41-3 (±)-ethyl 2-amino-3-(4-fluorophenyl)propanoate 
• 123286-12-4 Boc-DL-(p-fluoro)Phe-NH₂ 
• 1426814-68-7 (2R)-2-bromo-3-(4-fluorophenyl)propanoic acid 

Relevant academic research and scientific papers

Bi-enzymatic Conversion of Cinnamic Acids to 2-Arylethylamines

The conversion of carboxylic acids, such as acrylic acids, to amines is a transformation that remains challenging in synthetic organic chemistry. Despite the ubiquity of similar moieties in natural metabolic pathways, biocatalytic routes seem to have been overlooked for this purpose. Herein we present the conception and optimisation of a two-enzyme system, allowing the synthesis of β-phenylethylamine derivatives from readily-available ring-substituted cinnamic acids. After characterisation of both parts of the reaction in a two-step approach, a set of conditions allowing the one-pot biotransformation was optimised. This combination of a reversible deaminating and irreversible decarboxylating enzyme, both specific for the amino acid intermediate in tandem, represents a general method by which new strategies for the conversion of carboxylic acids to amines could be designed.

Organocatalytic Enantioselective Addition of α-Aminoalkyl Radicals to Isoquinolines

With a dual organocatalytic system involving a chiral phosphoric acid and a dicyanopyrazine-derived chromophore (DPZ) photosensitizer and under the irradiation with visible light, an enantioselective Minisci-type addition of α-amino acid-derived redox-active esters (RAEs) to isoquinolines has been developed. A variety of prochiral α-aminoalkyl radicals generated from RAEs were successfully introduced on isoquinolines, providing a range of valuable α-isoquinoline-substituted chiral secondary amines in high yields with good to excellent enantioselectivities.

ANTIBACTERIALS AND/OR MODULATORS OF BIOFILM FORMATION AND METHODS OF USING THE SAME

Amides substituted with aromatic groups were synthesized and some were purified to create enantiomer pure compounds. The compounds were tested to determine their ability to inhibit the growth of bacteria and the formation of biofilms created by bacteria. Some of these compounds were found to be effective antibacterials and to effectively inhibit the formation of biofilms.

Phenylalanine ammonia lyase catalyzed synthesis of amino acids by an MIO-cofactor independent pathway

Phenylalanine ammonia lyases (PALs) belong to a family of 4-methylideneimidazole-5-one (MIO) cofactor dependent enzymes which are responsible for the conversion of L-phenylalanine into trans-cinnamic acid in eukaryotic and prokaryotic organisms. Under conditions of high ammonia concentration, this deamination reaction is reversible and hence there is considerable interest in the development of PALs as biocatalysts for the enantioselective synthesis of non-natural amino acids. Herein the discovery of a previously unobserved competing MIO-independent reaction pathway, which proceeds in a non-stereoselective manner and results in the generation of both L- and D-phenylalanine derivatives, is described. The mechanism of the MIO-independent pathway is explored through isotopic-labeling studies and mutagenesis of key active-site residues. The results obtained are consistent with amino acid deamination occurring by a stepwise E1cB elimination mechanism. All manner of things: A competing MIO-independent (MIO=4-methylideneimidazole-5-one) reaction pathway has been identified for phenylalanine ammonia lyases (PALs), which proceeds in a non-stereoselective manner, resulting in the generation of D-phenylalanine derivatives. The mechanism of D-amino acid formation is explored through isotopic-labeling studies and mutagenesis of key active-site residues.

Immunomodulatory peptides

The invention relates to peptides derivatized with a hydrophilic polymer which, in some embodiments, bind to human FcRn and inhibit binding of the Fc portion of an IgG to an FcRn, thereby modulating serum IgG levels. The disclosed compositions and methods may be used in some embodiments, for example, in treating autoimmune diseases and inflammatory disorders. The invention also relates, in further embodiments, to methods of using and methods of making the peptides of the invention.

Enhanced reduction of C-N multiple bonds using sodium borohydride and an amorphous nickel catalyst

Amorphous nickel powder (Ni0) was utilised as a catalyst under mild, aqueous, basic conditions for enhancing the sodium borohydride-mediated reduction of C-N multiple bonds such as oximes, imines, hydrazones and nitriles to produce the corresponding amines in good to excellent yields.