35455-21-1

Usage

Uses

Used in Pharmaceutical Synthesis:
(R)-2-Amino-3-fluoropropanoic acid is used as a key intermediate in the synthesis of various pharmaceuticals. Its unique structural properties make it valuable for creating new compounds with potential therapeutic properties.
Used in Medicinal Chemistry:
In the field of medicinal chemistry, (R)-2-Amino-3-fluoropropanoic acid is used as a building block for the production of biologically active molecules. Its versatile reactivity allows for the development of innovative compounds with potential applications in healthcare.
Used in Agrochemical Production:
(R)-2-Amino-3-fluoropropanoic acid is also utilized in the production of agrochemicals, where its unique structure and reactivity contribute to the development of effective products for agricultural applications.
Used in Specialty Chemicals:
Furthermore, (R)-2-Amino-3-fluoropropanoic acid is employed in the production of specialty chemicals, showcasing its broad range of applications across different industries.

Upstream product

• 56-45-1 L-serin 
• 918409-09-3 (4R)-4-fluoromethyl-5-oxo-oxazolidine-3-carboxylic acid benzyl ester 
• 2923-22-0 β-fluoropyruvic acid sodium salt 
• 433-48-7 fluoropyruvic acid 
• 16652-37-2 3-fluoroalanine 
• 76312-98-6 3-fluoro-L-alanine methyl ester 
• 52-89-1 l-cysteine hydrochloride 

Downstream Products

• 76312-98-6 3-fluoro-L-alanine methyl ester 
• 76399-81-0 L-t-BOC-3-fluoroalanine 
• 36369-34-3 (2R)-2-benzyloxycarbonylamino-3-fluoropropionic acid 

Relevant academic research and scientific papers

Sustainable and Continuous Synthesis of Enantiopure l-Amino Acids by Using a Versatile Immobilised Multienzyme System

The enzymatic synthesis of α-amino acids is a sustainable and efficient alternative to chemical processes, through which achieving enantiopure products is difficult. To more address this synthesis efficiently, a hierarchical architecture that irreversibly co-immobilises an amino acid dehydrogenase with polyethyleneimine on porous agarose beads has been designed and fabricated. The cationic polymer acts as an irreversible anchoring layer for the formate dehydrogenase. In this architecture, the two enzymes and polymer colocalise across the whole microstructure of the porous carrier. This multifunctional heterogeneous biocatalyst was kinetically characterised and applied to the enantioselective synthesis of a variety of canonical and noncanonical α-amino acids in both discontinuous (batch) and continuous modes. The co-immobilised bienzymatic system conserves more than 50 % of its initial effectiveness after five batch cycles and 8 days of continuous operation. Additionally, the environmental impact of this process has been semiquantitatively calculated and compared with the state of the art.

Synthesis and use of N-Fmoc-l-fluoroalanine

We report a practical synthesis of N-Fmoc protected l-fluoroalanine 6 from l-serine. The key step involves a deoxofluorination reaction which was best achieved using XtalFluor-E in the presence of triethylamine trihydrofluoride. We also report the use of 6 in solid-phase peptide synthesis for the preparation of a model tripeptide demonstrating the possibility of incorporating a fluorinated probe in a peptide without elimination. Furthermore, cleavage of the dipeptide permitted to verify that 6 has a high enantiopurity.

ω-Transaminase-catalyzed asymmetric synthesis of unnatural amino acids using isopropylamine as an amino donor

Isopropylamine is an ideal amino donor for reductive amination of carbonyl compounds by ω-transaminase (ω-TA) owing to its cheapness and high volatility of a ketone product. Here we developed asymmetric synthesis of unnatural amino acids via ω-TA-catalyzed amino group transfer between α-keto acids and isopropylamine.

Kinetic resolution of 3-fluoroalanine using a fusion protein of D-amino acid oxidase with Vitroscilla hemoglobin

In this study, a fusion protein (VHb-DAAO) of D-amino acid oxidase (DAAO) with Vitreoscilla hemoglobin (VHb) was functionally expressed in Escherichia coli and purified. The kcat value VHb-DAAO (47.1 s-1) towards rac-3-flouroalanine was about 2-fold higher than that of DAAO (21.9 s -1). rac-3-Flouroalanine (500 mm) was kinetically resolved into (R)-3-fluoroalanine with high enatiomeric excess (>99%) by VHb-DAAO with about 52% conversion.

Thermodynamics and kinetic aspects involved in the enzymatic resolution of (R,S)-3-fluoroalanine in a coupled system of redox reactions catalyzed by dehydrogenases

Two systems of redox enzymatic reactions were tested, looking forward to the preparation of (S)-3-fluoroalanine, a potent antibiotic, by kinetic resolution of rac-3-fluoroalanine. This starting material was the main substrate for the deaminative oxidation reaction catalyzed by L-alanine dehydrogenase (L-AlaDH) in the presence of NAD+. One system was formed by coupling this reaction (main reaction) to the reduction of 3-fluoropyruvate (a cascade system) produced in the main reaction catalyzed by L-lactate dehydrogenase (L-LDH) in the presence of NADH, also formed in the main reaction. This system, that was able to achieve 92% of conversion, allows the accumulation of NH 4+, one of the secondary products of the main reaction. The other coupled redox system involved the coupling to the L-AlaDH reaction to the aminative reduction reaction of α-ketoglutarate in the presence of NADH and NH4+ (both side products of the main reaction) catalyzed by L-glutamate dehydrogenase (L-GluDH), that allows accumulation of 3-fluoropyruvate. With this system, the extent of the reaction in the coupled system was only 22%. This big difference in the efficiency of both systems was identified as being the result of a different potency of the products that accumulates in both systems, acting as inhibitors of L-AlaDH. It was demonstrated that 3-fluoropyruvate is a much stronger inhibitor of L-AlaDH than NH4+. This fact, and not thermodynamic considerations, explains the results obtained with both systems.

Kinetic aspects involved in the simultaneous enzymatic synthesis of (S)-3-fluoroalanine and (R)-3-fluorolactic acid

Desaminative oxidation of rac -3-fluoroalanine (rac-1) catalyzed by l-alanine dehydrogenase (l-ALADH) was studied by means of initial rate experiments both in the presence and in the absence of a product. Estimates of kinetic parameters of the reaction were obtained. The reaction mechanism is the sequential ordered BiTer mechanism with inhibition by excess of (S)-3-fluoroalanine. This kinetic study was the basis for the development of a couple enzymatic system for the simultaneous synthesis of (S)-3-fluoroalanine (1a) and (R)-3-fluorolactic acid (3) with l-ALADH and l-lactate dehydrogenase using rac-1 and NAD+. Analysis of isolated products revealed 1a in 60% yield and 86% ee and 3 in 80% yield and over 99% ee. Compounds 1a and 3 represent chiral building blocks for the synthesis of several products with pharmacological activity. The presence of the fluorine atom in the substrate causes a better interaction of it in the active site of the enzyme.

SYNTHESIS AND ENZYMATIC CLEAVAGE OF D,L-3-FLUOROALANINE

The action of bromine trifluoride on methyl 2,3-dibromopropionate in the presence of stannic chloride gives a high yield of methyl 2-bromo-3-fluoropropionate.Under the conditions of phase-transfer catalysis the product gave a 3-fluoro-2-azido ester, and reduction of the latter with hydrogen in the presence of Pd/C gave 3-fluoroalanine methyl ester.Enzymatic cleavage of N-BOC-3-fluoro-D,L-alanine methyl ester with papain took place stereospecifically, and N-BOC-3-fluoro-L-alanine was isolated with an almost quantitative yield.

THE MECHANISM OF SERINE FLUORODEHYDROXYLATION: 13C AND 19F NMR STUDIES

Competitive reaction pathways responsible for the incomplete fluorination of serine by SF4 were elucidated and inhibited.

Fluorinated amino acids

Deutero analogs of 3-fluoro-D-alanine prepared by direct photofluorination of the D-amino acids demonstrate in vivo and in vitro antibacterial activity against both gram negative and gram positive microorganisms. Deuters analogs of 3-fluoro-L-alanine and 3-fluoro-D,L-alanine also demonstrate useful in vitro activity.

Fluorodesulfurization of alkyl mercaptans or alkyl dithianes

Organic compounds containing a mercapto group or a dithiane moiety can be transformed into the analogous fluoro or difluoro compounds by reacting them with a halogenating reagent in liquid hydrogen fluoride, optionally containing boron trifluoride or antimony pentafluoride solution, at temperatures from about -80° and 15° C. The method may be descriptively termed "fluorodesulfurization".