Product Overview

5-Fluoro-L-tryptophan, also known as L-5-fluorotryptophan or 5-F-Trp, is a non-canonical amino acid derived from L-tryptophan by introducing a fluorine atom at the 5-position of the indole ring. As a fluorinated tryptophan analog and fluorinated indole amino acid, it is useful for protein research, peptide synthesis, enzyme mechanism studies, and metabolic research.

5-Fluoro-L-tryptophan is particularly valuable for ^19F NMR protein labeling and unnatural amino acid incorporation, providing a fluorinated residue for investigating protein structure, conformational changes, molecular interactions, and enzyme activity.

Hzymes produces 5-Fluoro-L-tryptophan through an enzymatic synthesis process, in which tryptophan synthase catalyzes the condensation of 5-fluoroindole with L-serine under aqueous conditions. The biocatalytic synthesis route provides high stereochemical selectivity while reducing reliance on conventional chemical synthesis methods.

With HPLC purity ≥99%, single impurity ≤0.5%, and optical purity ee ≥99.9%, Hzymes 5-Fluoro-L-tryptophan is suitable for research applications requiring a high-purity non-canonical amino acid building block.

Key Features

High-Purity Non-Canonical Amino Acid

Hzymes 5-Fluoro-L-tryptophan is manufactured with controlled chemical and optical purity to support reliable and reproducible research.

• HPLC purity ≥99%

• Single impurity ≤0.5%

• Optical purity ee ≥99.9%

• Batch-specific COA available

For researchers seeking a reliable non-canonical amino acid supplier, Hzymes provides 5-Fluoro-L-tryptophan for protein engineering, peptide synthesis, NMR studies, and biocatalysis.

High Optical Purity

The enzymatic synthesis route provides high stereochemical selectivity without conventional chiral resolution.

With ee ≥99.9%, the product is suitable for applications where stereochemical purity is important, including unnatural amino acid incorporation and peptide synthesis.

Enzymatic and Aqueous Synthesis

5-Fluoro-L-tryptophan is produced through an enzyme-catalyzed synthesis route using tryptophan synthase.

The biocatalytic synthesis of fluorotryptophan is performed under aqueous conditions and provides high stereochemical selectivity, supporting the preparation of high-purity fluorinated amino acid building blocks.

Consistent Batch Quality

Key quality attributes are controlled to support consistent product performance across batches.

• Controlled chemical purity

• High optical purity

• Controlled impurity profile

• Water content ≤1%

• Batch-specific Certificate of Analysis

Applications

19F NMR Protein Labeling

5-Fluoro-L-tryptophan can be incorporated into recombinant proteins as an analogue of natural tryptophan.

The fluorine atom provides a sensitive NMR signal with minimal biological background, allowing 5-Fluoro-L-tryptophan to function as a fluorotryptophan NMR probe for studying protein structure and dynamics.

Potential applications include:

• 19F NMR protein labeling

• Protein conformational analysis

• Protein dynamics studies

• Ligand-binding studies

• Enzyme mechanism research

• Molecular interaction studies

Unnatural Amino Acid Incorporation

As a non-canonical amino acid, 5-Fluoro-L-tryptophan can be used in research involving unnatural amino acid incorporation and protein engineering.

Its fluorinated indole structure provides an additional chemical and spectroscopic handle for investigating:

• Protein structure

• Protein dynamics

• Enzyme activity

• Molecular recognition

• Protein–ligand interactions

5-Fluorotryptophan Peptide Synthesis

5-Fluoro-L-tryptophan can be incorporated into peptides to investigate how fluorination affects peptide structure, stability, and biological activity.

Applications include:

• 5-fluorotryptophan peptide synthesis

• Fluorinated peptide design

• Structure–activity relationship studies

• Fluorinated antimicrobial peptides

• Cyclic and macrocyclic peptide research

• Peptide lead optimization

Protected derivatives such as Fmoc-5-Fluoro-L-tryptophan and Boc-5-Fluoro-L-tryptophan can serve as building blocks for solid-phase peptide synthesis, depending on the synthesis strategy.

Metabolic Research

5-Fluoro-L-tryptophan can be used as a fluorinated tryptophan analog in research investigating tryptophan metabolism and enzyme activity.

Potential applications include:

• Tryptophan metabolic pathway studies

• Metabolic flux research

• Enzyme substrate studies

• IDO-related research

• Fluorinated amino acid metabolism

• 5-fluorotryptophan metabolic stability studies

Enzyme Mechanism and Biocatalysis

5-Fluoro-L-tryptophan can serve as a substrate analogue in research involving tryptophan synthase and related enzymes.

It can support studies of:

• Substrate recognition

• Enzyme specificity

• Catalytic mechanisms

• Enzyme engineering

• Tryptophan synthase variants

• Biocatalytic synthesis of fluorotryptophan

Performance Data

Quality Assessment Conforms to product quality specifications

LC-MS Consistent with the expected molecular mass

¹H NMR Consistent with the expected chemical structure

Enantiomeric Purity (ee) 100%

FAQ

What is 5-Fluoro-L-tryptophan?

5-Fluoro-L-tryptophan is a fluorinated, non-canonical amino acid derived from L-tryptophan by introducing fluorine at the 5-position of the indole ring. It is also known as L-5-fluorotryptophan or 5-F-Trp.

What is 5-Fluoro-L-tryptophan used for?

5-Fluoro-L-tryptophan is used in research involving ^19F NMR protein labeling, unnatural amino acid incorporation, 5-fluorotryptophan peptide synthesis, protein structure studies, metabolic research, enzyme mechanism studies, and biocatalysis.

Can 5-Fluoro-L-tryptophan be used for ^19F NMR?

Yes. 5-Fluoro-L-tryptophan can be incorporated into proteins and used as a fluorotryptophan NMR probe for investigating protein structure, conformational changes, dynamics, and molecular interactions.

Can 5-Fluoro-L-tryptophan be used for peptide synthesis?

Yes. 5-Fluoro-L-tryptophan can be used as a fluorinated amino acid building block for peptide synthesis. Fmoc- and Boc-protected derivatives can also be used depending on the synthesis strategy.

What is the purity of Hzymes 5-Fluoro-L-tryptophan?

The product specification includes HPLC purity ≥99%, single impurity ≤0.5%, and optical purity ee ≥99.9%.

How is 5-Fluoro-L-tryptophan synthesized?

Hzymes produces 5-Fluoro-L-tryptophan through an enzyme-catalyzed synthesis process using tryptophan synthase to catalyze the condensation of 5-fluoroindole with L-serine under aqueous conditions.

Can 5-Fluoro-L-tryptophan be used for unnatural amino acid incorporation?

Yes. As a non-canonical amino acid, 5-Fluoro-L-tryptophan can be used in research involving unnatural amino acid incorporation, protein engineering, and fluorine-based protein analysis.

Is 5-Fluoro-L-tryptophan available in protected forms?

Fmoc-5-Fluoro-L-tryptophan and Boc-5-Fluoro-L-tryptophan may be available depending on project requirements. Please contact Hzymes for availability, specifications, and customization options.

How should 5-Fluoro-L-tryptophan be stored?

Store the product in a cool, dry place and protect it from light and moisture. Keep the container tightly closed after use. For detailed storage conditions, please refer to the product specification and COA.