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Usage

Uses

Used in Pharmaceutical Industry:
(R)-2-Amino-3-(3,4,5-trifluoro-phenyl)-propionic acid is used as an intermediate in the synthesis of various pharmaceutical compounds. The presence of the fluorine atoms and the chiral center in the molecule can contribute to the development of new drugs with improved properties, such as enhanced bioavailability, increased stability, and better target specificity.
Used in Agrochemical Industry:
(R)-2-Amino-3-(3,4,5-trifluoro-phenyl)-propionic acid is used as a building block in the creation of agrochemicals, such as pesticides and herbicides. The unique properties conferred by the fluorine atoms can lead to the development of more effective and environmentally friendly agrochemicals with reduced toxicity and increased selectivity towards target pests or weeds.
Used in Materials Science:
(R)-2-Amino-3-(3,4,5-trifluoro-phenyl)-propionic acid can be utilized in the development of novel materials with specific properties, such as improved thermal stability, enhanced chemical resistance, or increased mechanical strength. The incorporation of (R)-2-AMINO-3-(3,4,5-TRIFLUORO-PHENYL)-PROPIONIC ACID into polymers or other materials can lead to the creation of advanced materials for various applications, including electronics, automotive, and aerospace industries.

Upstream product

• 261952-26-5 C₉H₈F₃NO₂ 
• 324027-94-3 diethyl 2-acetamido-2-(3,4,5-trifluorobenzyl)malonate 
• 324028-00-4 2-acetylamino-2-(3,4,5-trifluoro-benzyl)-malonic acid 
• 324028-06-0 acetyl-DL-3,4,5-trifluorophenylalanine 
• 220141-72-0 3,4,5-trifluorobenzyl bromide 
• 324028-12-8 acetyl-D-3,4,5-trifluorophenylalanine 

Downstream Products

• 1227832-70-3 C₂₀H₁₄F₃NO₃ 

Relevant academic research and scientific papers

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.

Exploration of the role of phenylalanine in the thrombin receptor tethered-ligand peptide by substitution with a series of trifluorophenylalanines

The thrombin receptor-tethered ligand SFLLRNP (abbreviation formed by one letter amino acid codes expressing Ser-Phe-Leu-Leu-Arg-Asn-Pro) consists of the Phe-2 residue essential for the receptor activation. In order to explore the molecular characteristics of this Phe-2-phenyl, a series of trifluorophenylalanines [(F3)Phe] was incorporated into this S/Phe/LLRNP for evaluation of their ability to induce the human platelet aggregation. A complete set of (F3)Phe in the L-configuration, namely, (2,3,4-F3)Phe, (2,3,5-F3)Phe, (2,3,6-F3)Phe, (2,4,5-F3)Phe, (2,4,6-F3)Phe, and (3,4,5-F3)Phe, was prepared from trifluorobenzyl bromides and diethyl acetamidomalonate. S/(2,3,4-F3)Phe/LLRNP was equipotent to S/Phe/LLRNP, while (2,4,5-F3)Phe-containing analog was almost twice as potent as those. (2,4,6-F3)Phe-analog exhibited about a half of the activity of S/Phe/LLRNP. (3,4,5-F3)Phe-, (2,3,5-F3)Phe-, and (2,3,6-F3)Phe-analogs were very weak. The analysis of these assay results suggested that Phe-2-phenyl of SFLLRNP is in the edge-to-face CH/π interaction with the receptor aromatic group, utilizing the Phe-2-phenyl edge along with benzene hydrogens at position 2-3 or 5-6. The computer-assisted semi-empirical molecular orbital calculations by MOPAC showed that the fluorine atom decreases the electron density of its ortho, meta, and para hydrogens, and thus increases their acidity more strongly in that order. All these suggested that H → F replacements reinforce the edge-to-face CH/π interaction to enhance biological activity. The H → F replacement on the Phe-phenyl group was found to render an effective structural examination; i.e., to identify the hydrogens in the CH/π interaction, and to intensify the CH/π interaction.