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3-Fluoro-DL-phenylalanine is a chemical compound that is structurally similar to the naturally occurring amino acid phenylalanine, with a key difference being the substitution of a fluorine atom for one of the hydrogen atoms. This racemic mixture contains equal parts of both the D and L enantiomers, offering unique properties and applications in various fields.

456-88-2

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456-88-2 Usage

Uses

Used in Pharmaceutical Industry:
3-Fluoro-DL-phenylalanine serves as a chiral building block, playing a crucial role in the synthesis of a variety of drugs and pharmaceuticals. Its unique structure allows for the creation of new compounds with distinct properties and therapeutic effects.
Used in Research and Development:
As a tool for studying the effects of fluorine substitution on the biological activity of amino acids, 3-fluoro-DL-phenylalanine aids researchers in understanding how such substitutions can influence the properties and functions of amino acids in biological systems.
Used in Drug Development:
3-Fluoro-DL-phenylalanine holds potential in the development of new drugs for the treatment of various diseases and conditions. Its incorporation into drug molecules can lead to improved pharmacokinetics, enhanced target specificity, and increased therapeutic efficacy.

Check Digit Verification of cas no

The CAS Registry Mumber 456-88-2 includes 6 digits separated into 3 groups by hyphens. The first part of the number,starting from the left, has 3 digits, 4,5 and 6 respectively; the second part has 2 digits, 8 and 8 respectively.
Calculate Digit Verification of CAS Registry Number 456-88:
(5*4)+(4*5)+(3*6)+(2*8)+(1*8)=82
82 % 10 = 2
So 456-88-2 is a valid CAS Registry Number.
InChI:InChI=1/C9H10FNO2/c10-7-3-1-2-6(4-7)5-8(11)9(12)13/h1-4,8H,5,11H2,(H,12,13)

456-88-2 Well-known Company Product Price

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  • TCI America

  • (F0169)  3-Fluoro-DL-phenylalanine  >98.0%(HPLC)(T)

  • 456-88-2

  • 1g

  • 450.00CNY

  • Detail
  • TCI America

  • (F0169)  3-Fluoro-DL-phenylalanine  >98.0%(HPLC)(T)

  • 456-88-2

  • 5g

  • 1,990.00CNY

  • Detail
  • Sigma

  • (F5126)  m-Fluoro-DL-phenylalanine  

  • 456-88-2

  • F5126-5G

  • 2,091.96CNY

  • Detail

456-88-2SDS

SAFETY DATA SHEETS

According to Globally Harmonized System of Classification and Labelling of Chemicals (GHS) - Sixth revised edition

Version: 1.0

Creation Date: Aug 11, 2017

Revision Date: Aug 11, 2017

1.Identification

1.1 GHS Product identifier

Product name m-Fluoro-DL-phenylalanine

1.2 Other means of identification

Product number -
Other names 3-FLUORO-DL-PHENYLALANINE

1.3 Recommended use of the chemical and restrictions on use

Identified uses For industry use only.
Uses advised against no data available

1.4 Supplier's details

1.5 Emergency phone number

Emergency phone number -
Service hours Monday to Friday, 9am-5pm (Standard time zone: UTC/GMT +8 hours).

More Details:456-88-2 SDS

456-88-2Relevant academic research and scientific papers

Bi-enzymatic Conversion of Cinnamic Acids to 2-Arylethylamines

Weise, Nicholas J.,Thapa, Prasansa,Ahmed, Syed T.,Heath, Rachel S.,Parmeggiani, Fabio,Turner, Nicholas J.,Flitsch, Sabine L.

, p. 995 - 998 (2020/01/21)

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.

Exploring the tetrahydroisoquinoline thiohydantoin scaffold blockade the androgen receptor as potent anti-prostate cancer agents

Xu, Xi,Ge, Raoling,Li, Lei,Wang, Jubo,Lu, Xiaoyu,Xue, Siqi,Chen, Xijing,Li, Zhiyu,Bian, Jinlei

, p. 1325 - 1344 (2017/11/13)

Prostate cancer (PC) is a major cause of cancer-related male death in worldwide and the identification of new and improved potent anti-PC molecules is constantly required. A novel scaffold of tetrahydroisoquinoline thiohydantoin was rationally designed based on the enzalutamide structures and our pre-work, leading to the discovery of a series of new antiproliferative compounds. Several new analogues displayed improved androgen receptor (AR) antagonistic activity, while maintaining the higher selective toxicity toward LNCaP cells (AR-rich) versus DU145 cells (AR-deficient) compared to enzalutamide. In fact, compound 55 exhibited promising in vitro antitumor activity by impairing AR unclear translocation. More importantly, 55 showed better pharmacokinetic properties compared to the compound 1 reported in our pre-work. These results demonstrate a step towards the development of novel and improved AR antagonists.

Organocatalytic Enantioselective Addition of α-Aminoalkyl Radicals to Isoquinolines

Liu, Xiangyuan,Liu, Yang,Chai, Guobi,Qiao, Baokun,Zhao, Xiaowei,Jiang, Zhiyong

supporting information, p. 6298 - 6301 (2018/10/09)

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

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Paragraph 0087; 0089; 0092, (2017/04/11)

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

Lovelock, Sarah L.,Lloyd, Richard C.,Turner, Nicholas J.

supporting information, p. 4652 - 4656 (2014/05/20)

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.

Enantioselective synthesis of non-natural amino acids using phenylalanine dehydrogenases modified by site-directed mutagenesis

Busca, Patricia,Paradisi, Francesca,Moynihan, Eamonn,Maguire, Anita R.,Engel, Paul C.

, p. 2684 - 2691 (2007/10/03)

The substrate scope of three mutants of phenylalanine dehydrogenase as biocatalysts for the transformation of a series of 2-oxo acids, structurally related to phenylpyruvic acid, to the analogous -amino acids, non-natural analogues of phenylalanine, has been investigated. The mutant enzymes are more tolerant than the wild type enzyme of the non-natural substrates, especially those with substituents at the 4-position on the phenyl ring. Excellent enantiocontrol resulted in all cases.

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