108391-82-8

Basic information

• Product Name: 6-fluoro-D-tryptophan
• Synonyms: 6-fluoro-D-tryptophan;D-Tryptophan, 6-fluoro-;(R)-2-Amino-3-(6-fluoro-1H-indol-3-yl)propanoic acid
• CAS NO: 108391-82-8
• Molecular Formula: C11H11FN2O2
• Molecular Weight: 222.2156432
• EINECS: -0
• Mol File: 108391-82-8.mol

Chemical Properties

• Appearance: /
• CAS DataBase Reference: 6-fluoro-D-tryptophan(CAS DataBase Reference)
• NIST Chemistry Reference: 6-fluoro-D-tryptophan(108391-82-8)
• EPA Substance Registry System: 6-fluoro-D-tryptophan(108391-82-8)

Safety Data

• Hazardous Substances Data: 108391-82-8(Hazardous Substances Data)

Usage

Uses

Used in Pharmaceutical Research:
6-fluoro-D-tryptophan is utilized as a research tool for investigating the role of tryptophan in various biological processes. The fluorine substitution can affect the compound's binding affinity and metabolic pathways, providing insights into the mechanisms of action and potential therapeutic targets.
Used in Drug Development:
As a synthetic analog of tryptophan, 6-fluoro-D-tryptophan is employed in the development of new drugs targeting specific proteins and pathways. Its unique properties may offer advantages over native tryptophan, such as improved stability, selectivity, or potency, making it a promising candidate for the creation of novel therapeutic agents.
Used in Biochemical Studies:
6-fluoro-D-tryptophan serves as a valuable probe in biochemical studies, allowing researchers to explore the structural and functional aspects of tryptophan-containing proteins. The altered properties of the compound can reveal important information about protein-ligand interactions, enzyme mechanisms, and the role of tryptophan residues in protein function.
Used in Diagnostic Applications:
The distinct properties of 6-fluoro-D-tryptophan can be harnessed for the development of diagnostic tools and assays. Its unique binding characteristics and potential to modulate protein function may enable the detection and monitoring of specific biological processes or the presence of certain proteins in biological samples.
Used in Radiolabeling Techniques:
6-fluoro-D-tryptophan can be employed in radiolabeling techniques for imaging and tracking purposes. The incorporation of a fluorine-18 isotope allows for the use of positron emission tomography (PET) to visualize the distribution and metabolism of the compound in living organisms, providing valuable information for research and clinical applications.
Used in Chemical Synthesis:
6-fluoro-D-tryptophan can be used as a building block in the synthesis of more complex molecules, such as peptidomimetics or other bioactive compounds. Its unique properties may contribute to the development of novel chemical entities with potential applications in various fields, including medicine, agriculture, and materials science.

Upstream product

• 50-00-0 formaldehyd 
• 154-08-5 DL-5-fluorotryptophan 
• 81024-49-9 N^α-acetyl-6-fluoro-D,L-tryptophan 
• 7730-20-3 DL-6-fluorotryptophan 
• 399-51-9 6-fluoro-1H-indole 
• 56-45-1 L-serin 

Downstream Products

• 108391-82-8 D-6-fluorotryptophan 
• 871498-18-9 2-amino-3-(6-fluoro-1H-indol-3-yl)-propionic acid methyl ester 
• 1234870-95-1 t-butoxycarbonyl-DL-6-fluorotryptophan 
• 67308-25-2 2-((tert-butoxycarbonyl)amino)-3-(6-fluoro-1H-indol-3-yl)propanoic acid 
• 461424-18-0 7-fluoro-1-(2-fluoro-phenyl)-9H-β-carboline 

Relevant articles and documents

Complete Stereoinversion of l -Tryptophan by a Fungal Single-Module Nonribosomal Peptide Synthetase

Single-module nonribosomal peptide synthetases (NRPSs) and NRPS-like enzymes activate and transform carboxylic acids in both primary and secondary metabolism and are of great interest due to their biocatalytic potentials. The single-module NRPS IvoA is essential for fungal pigment biosynthesis. Here, we show that IvoA catalyzes ATP-dependent unidirectional stereoinversion of l-tryptophan to d-tryptophan with complete conversion. While the stereoinversion is catalyzed by the epimerization (E) domain, the terminal condensation (C) domain stereoselectively hydrolyzes d-tryptophanyl-S-phosphopantetheine thioester and thus represents a noncanonical C domain function. Using IvoA, we demonstrate a biocatalytic stereoinversion/deracemization route to access a variety of substituted d-tryptophan analogs in high enantiomeric excess.

One-Pot Biocatalytic Synthesis of Substituted d -Tryptophans from Indoles Enabled by an Engineered Aminotransferase

d-Tryptophan and its derivatives are important precursors of a wide range of indole-containing pharmaceuticals and natural products. Here, we developed a one-pot biocatalytic process enabling the synthesis of d-tryptophans from indoles in good yields and high enantiomeric excess (91% to >99%). Our method couples the synthesis of l-tryptophans catalyzed by Salmonella enterica tryptophan synthase with a stereoinversion cascade mediated by Proteus myxofaciens l-amino acid deaminase and an aminotransferase variant that we engineered to display native-like activity toward d-tryptophan. Our process is applicable to preparative-scale synthesis of a broad range of d-tryptophan derivatives containing electron-donating or -withdrawing substituents at all benzene-ring positions on the indole group.

Regioselective enzymatic halogenation of substituted tryptophan derivatives using the FAD-dependent halogenase RebH

Regioselective methods to establish carbon-halide bonds are still rare, although halogenation is considered as a commonly used methodology for the functionalization of organic compounds. The incorporation of halogen substituents by organic synthesis usually requires hazardous conditions, shows poor regioselectivity and results in the formation of unwanted byproducts. In addition, halogenation by electrophilic aromatic substitution (SEAr) obeys distinct rules depending on electron-withdrawing or -donating groups already present in the aromatic ring. We employed the tryptophan-7-halogenase RebH for regioselective enzymatic halogenation to overcome these limitations. In combination with a tryptophan synthase, an array of C5- and C6-substituted tryptophan derivatives was synthesized and halogenated by RebH. The halogenase is able override these directing effects and halogenates at the electronically unfavored C7-meta-position, even in presence of ortho/para-directing groups. No business as usual: The tryptophan halogenase RebH from Lechevalieria aerocolonigenes is able to halogenate at the electronically unfavored C7-meta-position of C5-substituted tryptophan derivatives, even in presence of deactivating ortho/para-directing groups.

METHODS FOR PRODUCING D-TRYPTOPHAN AND SUBSTITUTED D-TRYPTOPHANS

Single-module nonribosomal peptide synthetases (NRPSs) and NRPS-like enzymes activate and transform carboxylic acids in both primary and secondary metabolism; and are of great interest due to their biocatalytic potentials. The single-module NRPS IvoA is essential for fungal pigment biosynthesis. As disclosed herein, we show that IvoA catalyzes ATP-dependent unidirectional stereoinversion of L-tryptophan to D-tryptophan with complete conversion. While the stereoinversion is catalyzed by the epimerization (E) domain, the terminal condensation (C) domain stereoselectively hydrolyzes D-tryptophanyl-S-phosphopantetheine thioester and thus represents a noncanonical C domain function. Using IvoA, we demonstrate a biocatalytic stereoinversion/deracemization route to access a variety of substituted D-tryptophan analogs in high enantiomeric excess.

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.

Synthesis of tripeptides containing d-Trp substituted at the indole ring, assessment of opioid receptor binding and in vivo central antinociception

The noncationizable tripeptide Ac-d-Trp-Phe-GlyNH2 was recently proposed as a novel minimal recognition motif for μ-opioid receptor. The introduction of different substituents (methyl, halogens, nitro, etc.) at the indole of d-Trp significantly influenced receptor affinities and resulted in serum stability and in a measurable effect on central antinociception in mice after ip administration.

The facile synthesis of a series of tryptophan derivatives

This study reports a facile method for the synthesis of a variety of 5- and 6-substituted tryptophan derivatives that are difficult to prepare using alternative enzymatic approaches. Acylation of an activated amino acid, derived from serine in situ, is coupled with an enzymatic resolution step to furnish enantiopure analogues bearing a range of electron withdrawing and releasing substituents. Isolation of a dehydroalanine derivative as a by-product from some reactions provides some insights into the likely mechanism of the reaction.

β-Carbolin-3-carboxylic acid derivatives

A β-carbolin-3-carboxylic acid derivative of the formula STR1 has valuable pharmacological properties when administered to patients, e.g. humans as a drug, have been shown to possess interesting tranquilizing activity.