82311-69-1

Basic information

• Product Name: 3-Bromo-L-phenylalanine
• Synonyms: 3-Bromo-L-phenylalanine;(S)-2-Amino-3-(3'-Bromophenyl)Propanoic Acid;(L)-Bromophenyl alanine;3-Br-L-Phe-OH;(S)-2-((3-bromophenyl)amino)propanoic acid;L-Phe(3-Br)-OH;m-Bromo-L-phenylalanine
• CAS NO: 82311-69-1
• Molecular Formula: C₉H₁₀BrNO₂
• Molecular Weight: 244.0852
• Product Categories: Amino Acids;Amino Acid Derivatives
• Mol File: 82311-69-1.mol

Chemical Properties

• Boiling Point: 368.4 °C at 760 mmHg
• Flash Point: 176.6 °C
• Appearance: /
• Density: 1.588 g/cm³
• Storage Temp.: Sealed in dry,Room Temperature
• PKA: 2.16±0.10(Predicted)
• Water Solubility: Slightly soluble in water.
• CAS DataBase Reference: 3-Bromo-L-phenylalanine(CAS DataBase Reference)
• NIST Chemistry Reference: 3-Bromo-L-phenylalanine(82311-69-1)
• EPA Substance Registry System: 3-Bromo-L-phenylalanine(82311-69-1)

Safety Data

• Hazardous Substances Data: 82311-69-1(Hazardous Substances Data)

Usage

Uses

Used in Pharmaceutical Industry:
3-Bromo-L-phenylalanine is used as a key intermediate in the synthesis of lifitegrast, a drug used for the treatment of dry eye syndrome. Its incorporation in the drug's structure contributes to its therapeutic effects, making it an essential component in the pharmaceutical industry.
Used in Biochemistry Research:
3-Bromo-L-phenylalanine is utilized in the facile removal of leader peptides from lanthipeptides through the incorporation of a hydroxy acid. This application aids researchers in studying the structure and function of lanthipeptides, which are a class of ribosomally synthesized and post-translationally modified peptides (RiPPs) with diverse biological activities.

Upstream product

• 82278-73-7 (2S)-3-(3-bromophenyl)-2-[(tert-butoxycarbonyl)amino]propanoic acid 
• 14473-91-7 3-Bromocinnamic acid 
• 14473-91-7 3-bromocinnamic acid 
• 3132-99-8 m-bromobenzoic aldehyde 
• 117391-50-1 3-amino-3-(3-bromo-phenyl)-propionic acid 
• 30163-20-3 2-amino-3-(3-bromophenyl)propanoic acid 

Downstream Products

• 82278-73-7 (2S)-3-(3-bromophenyl)-2-[(tert-butoxycarbonyl)amino]propanoic acid 
• 875782-96-0 C₁₀H₁₂BrNO₂ 
• 1289646-76-9 (S)-2-((tert-butoxycarbonyl)amino)-3-((3-methylsulfonyl)phenyl)propanol 
• 1289646-78-1 (S)-benzyl 2-((tert-butoxycarbonyl)amino)-3-((3-methylsulfonyl)phenyl)propionate 
• 1194550-59-8 (2S)-2-amino-3-(3-(methanesulfonyl)phenyl)propionic acid benzyl ester hydrochloride 
• 1194550-63-4 C₄₆H₄₀Cl₂N₂O₅S 
• 1194550-65-6 benzyl (S)-2-(5,7-dichloro-1,2,3,4-tetrahydroisoquinoline-6-carboxamido)-3-[3-(methylsulfonyl)phenyl]propanoate hydrochloride 
• 1194550-67-8 ((S)-benzyl 2-(2-(benzofuran-6-carbonyl)-5,7-dichloro-1,2,3,4-tetrahydroisoquinoline-6-carboxamido)-3-(3-methylsulfonyl)phenyl)propanoate 
• 1025967-78-5 (S)-2-(2-(benzofuran-6-carbonyl)-5,7-dichloro-1,2,3,4-tetrahydroisoquinoline-6-carboxamido)-3-(3-(methylsulfonyl)phenyl)propanoic acid 
• 164172-95-6 (S)-3-([1,1'-biphenyl]-3-yl)-2-aminopropanoic acid 

Relevant articles and documents

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.

Design, synthesis, and functional assessment of Cmpd-15 derivatives as negative allosteric modulators for the β2-adrenergic receptor

The β2-adrenergic receptor (β2AR), a G protein-coupled receptor, is an important therapeutic target. We recently described Cmpd-15, the first small molecule negative allosteric modulator (NAM) for the β2AR. Herein we report in details the design, synthesis and structure-activity relationships (SAR) of seven Cmpd-15 derivatives. Furthermore, we provide in a dose-response paradigm, the details of the effects of these derivatives in modulating agonist-induced β2AR activities (G-protein-mediated cAMP production and β-arrestin recruitment to the receptor) as well as the binding affinity of an orthosteric agonist in radio-ligand competition binding assay. Our results show that some modifications, including removal of the formamide group in the para-formamido phenylalanine region and bromine in the meta-bromobenzyl methylbenzamide region caused dramatic reduction in the functional activity of Cmpd-15. These SAR results provide valuable insights into the mechanism of action of the NAM Cmpd-15 as well as the basis for future development of more potent and selective modulators for the β2AR based on the chemical scaffold of Cmpd-15.

Kinetic Resolution of Aromatic β-Amino Acids Using a Combination of Phenylalanine Ammonia Lyase and Aminomutase Biocatalysts

An enzymatic strategy for the preparation of (R)-β-arylalanines employing phenylalanine aminomutase and ammonia lyase (PAM and PAL) enzymes has been demonstrated. Candidate PAMs with the desired (S)-selectivity from Streptomyces maritimus (EncP) and Bacillus sp. (PabH) were identified via sequence analysis using a well-studied template sequence. The newly discovered PabH could be linked to the first ever proposed biosynthesis of pyloricidin-like secondary metabolites and was shown to display better β-lyase activity in many cases. In spite of this, a method combining the higher conversion of EncP with a strict α-lyase from Anabaena variabilis (AvPAL) was found to be more amenable, allowing kinetic resolution of five racemic substrates and a preparative-scale reaction with >98% (R) enantiomeric excess. This work represents an improved and enantiocomplementary method to existing biocatalytic strategies, allowing simple product separation and modular telescopic combination with a preceding chemical step using an achiral aldehyde as starting material. (Figure presented.).

Intensified biocatalytic production of enantiomerically pure halophenylalanines from acrylic acids using ammonium carbamate as the ammonia source

An intensified, industrially-relevant strategy for the production of enantiopure halophenylalanines has been developed using the novel combination of a cyanobacterial phenylalanine ammonia lyase (PAL) and ammonium carbamate reaction buffer. The process boasts STYs up to >200 g L-1 d-1, ees ≥ 98% and simplified catalyst/reaction buffer preparation and work up.

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).

The bacterial ammonia lyase EncP: A tunable biocatalyst for the synthesis of unnatural amino acids

Enzymes of the class I lyase-like family catalyze the asymmetric addition of ammonia to arylacrylates, yielding high value amino acids as products. Recent examples include the use of phenylalanine ammonia lyases (PALs), either alone or as a gateway to deracemization cascades (giving (S)- or (R)-α-phenylalanine derivatives, respectively), and also eukaryotic phenylalanine aminomutases (PAMs) for the synthesis of the (R)-β-products. Herein, we present the investigation of another family member, EncP from Streptomyces maritimus, thereby expanding the biocatalytic toolbox and enabling the production of the missing (S)-β-isomer. EncP was found to convert a range of arylacrylates to a mixture of (S)-α- and (S)-β-arylalanines, with regioselectivity correlating to the strength of electron-withdrawing/-donating groups on the ring of each substrate. The low regioselectivity of the wild-type enzyme was addressed via structure-based rational design to generate three variants with altered preference for either α- or β-products. By examining various biocatalyst/substrate combinations, it was demonstrated that the amination pattern of the reaction could be tuned to achieve selectivities between 99:1 and 1:99 for β:α-product ratios as desired.

Phenylalanine aminomutase-catalyzed addition of ammonia to substituted cinnamic acids: A route to enantiopure α- and β-amino acids

(Chemical Equation Presented) An approach is described for the synthesis of aromatic α- and β-amino acids that uses phenylalanine aminomutase to catalyze a highly enantioselective addition of ammonia to substituted cinnamic acids. The reaction has a broad scope and yields substituted α- and β-phenylalanines with excellent enantiomeric excess. The regioselectivity of the conversion is determined by substituents present at the aromatic ring. A box model for the enzyme active site is proposed, derived from the influence of the hydrophobicity of substituents on the enzyme affinity toward various substrates.

THIAZOLE DERIVATIVES AS KINASE INHIBITORS

A series of thiazole derivatives which are substituted in the 2-position by a substituted morpholin-4-yl moiety, being selective inhibitors of P13 kinase enzymes, are accordingly of benefit in medicine, for example in the treatment of inflammatory, autoimmune, cardiovascular, neurodegenerative, metabolic, oncological, nociceptive or ophthalmic conditions.

FUSED THIAZOLE DERIVATIVES AS KINASE INHIBITORS

A series of 5,6-dihydro-l,3-benzothiazol-7(4H)-one derivatives, and analogues thereof, which are substituted in the 2-position by an optionally substituted morpholin-4-yl moiety, being selective inhibitors of PD kinase enzymes, are accordingly of b.enefit in medicine, for example in the treatment of inflammatory, autoimmune, cardiovascular, neurodegenerative, metabolic, oncological, nociceptive or ophthalmic conditions.

Pharmacologically active peptides

Compounds of the formula STR1 and pharmaceutically acceptable non-toxic acid addition salts thereof, in which R is hydrogen, methyl, ethyl, cyclopropylmethyl, or allyl; A is a residue of a D-amino acid selected from the group consisting of Ala, Abu, Nva, Val, Nle, Leu, Ile, Gly(Al), Gly(Cp), Met, Cys(Me), Met(O), Cys(Me) (O), Ser, Thr, and Hse; R1 is C1 -C3 primary alkyl, cyclopropylmethyl, allyl, ethylthiomethyl, 2-fluoroethyl, or propargyl; X is bromo, iodo, chloro, methyl, trifluoromethyl, or methoxy; and Z is --CH2 OR2, STR2 in which R2 is hydrogen, acetyl, or acetoxymethyl and R3 is C1 -C3 alkyl; are useful analgesic agents.