Product Overview

Fmoc-7-methyl-L-tryptophan is a non-canonical amino acid building block featuring a methyl group at the 7-position of the indole ring and an N-terminal 9-fluorenylmethoxycarbonyl (Fmoc) protecting group. As a 7-methyltryptophan unnatural amino acid, it provides researchers with a structurally differentiated tryptophan derivative for peptide design, medicinal chemistry, and structure–activity relationship (SAR) studies.

The product combines the functional characteristics of an indole methylated amino acid building block with the synthetic convenience of Fmoc protection. It is designed to be compatible with conventional Fmoc-SPPS, making it suitable for the preparation of modified peptides, peptide analogs, and other non-canonical amino acid peptide sequences.

Hzymes Biotech manufactures Fmoc-7-methyl-L-tryptophan using a combined enzymatic and chemical synthesis strategy. In the biocatalytic step, tryptophan synthase catalyzes the condensation of 7-methylindole with L-serine to produce 7-methyl-L-tryptophan, followed by Fmoc protection using Fmoc-OSu or Fmoc-Cl under alkaline conditions. This biocatalytic synthesis of 7-methyltryptophan supports efficient preparation of the desired L-configured amino acid.

The enzymatic platform can utilize engineered tryptophan synthase systems, including evolved TrpB 7-methylindole biocatalytic approaches, to support stereoselective amino acid synthesis.

The resulting Fmoc protected methyltryptophan is supplied as a white to off-white powder with high chemical and stereochemical purity. HPLC purity is ≥99.5%, with single impurity ≤0.5%, while optical purity reaches ee ≥99.9%. Each batch is supported by a Certificate of Analysis (CoA).

Product Specifications

• Product: Fmoc-7-methyl-L-tryptophan

• CAS No.: 1808268-53-2

• Molecular Formula: C₂₇H₂₄N₂O₄

• Molecular Weight: 440.49

• Appearance: White to off-white powder

• HPLC Purity: ≥99.5%

• Optical Purity: ≥99.9% ee

• Single Impurity: ≤0.5%

• Water Content: ≤1%

Key Features

High Chemical and Optical Purity

Fmoc-7-methyl-L-tryptophan is produced using a stereoselective enzymatic route, minimizing the need for conventional chiral resolution. Optical purity reaches ≥99.9% ee, making the product suitable for applications requiring tight stereochemical control.

The high-purity profile also makes it suitable for researchers looking for 7-methyltryptophan 99% ee or higher-purity modified amino acid building blocks.

Fmoc Protection for Standard SPPS

The Fmoc group enables direct integration into standard Fmoc-SPPS workflows. This product can therefore serve as an Fmoc NCAA SPPS compatible building block for incorporating a non-canonical tryptophan residue into peptide sequences.

Fmoc can be selectively removed under mild basic conditions, such as 20% piperidine in DMF, while preserving the side-chain methyl modification.

Enzymatic and Biocatalytic Manufacturing

The synthesis route combines enzymatic amino acid construction with chemical Fmoc protection. The use of tryptophan synthase provides a stereoselective route from 7-methylindole and L-serine, supporting the preparation of high-purity 7-methyltryptophan.

This approach is particularly relevant to researchers investigating 7-methylindole tryptophan synthase systems and engineered TrpB platforms for non-canonical amino acid production.

Consistent Batch Quality

Each batch is evaluated for key quality attributes, including appearance, HPLC purity, optical purity, impurities, water content, and residual solvents. Batch-specific analytical results are documented in the CoA to support reproducibility and traceability.

Applications

Non-Canonical Amino Acid Peptide Synthesis

Fmoc-7-methyl-L-tryptophan can be incorporated into peptide sequences as a non-canonical amino acid using standard Fmoc-SPPS protocols. It provides an alternative to natural tryptophan for investigating how targeted methyl substitution influences peptide properties.

The product is suitable for tryptophan derivative peptide synthesis, particularly when researchers need to introduce a defined structural modification while maintaining compatibility with established solid-phase synthesis workflows.

Peptide Drug Discovery and SAR Studies

The 7-methyl modification changes the steric and electronic environment of the indole ring and can be used to systematically investigate the influence of methyl substitution on peptide structure and biological activity.

In medicinal chemistry programs, this building block can support the design of methylated tryptophan peptide drug candidates and analog libraries for evaluating target affinity, selectivity, metabolic stability, and proteolytic resistance.

Macrocyclic Peptide Development

The product can also be considered for macrocyclic peptide methyltryptophan research, where incorporation of non-natural residues can help explore changes in conformation, hydrophobic interactions, and target recognition.

Its compatibility with Fmoc-SPPS makes it suitable for library-based synthesis and iterative optimization of modified and macrocyclic peptide candidates.

Peptide Structure and Molecular Interaction Studies

7-Methyl-L-tryptophan provides a useful molecular modification for investigating protein–peptide and protein–ligand interactions. Incorporation into peptide sequences can help researchers assess the contribution of the tryptophan indole ring to binding, conformation, and molecular recognition.

FAQ

Q1. What is Fmoc-7-methyl-L-tryptophan?

Fmoc-7-methyl-L-tryptophan is an Fmoc-protected 7-methyltryptophan derivative used as a non-canonical amino acid building block for peptide synthesis. A methyl group is introduced at the 7-position of the tryptophan indole ring.

Q2. Is Fmoc-7-methyl-L-tryptophan compatible with SPPS?

Yes. The product is designed for Fmoc-based solid-phase peptide synthesis (Fmoc-SPPS). It can be incorporated using conventional peptide coupling protocols, and the Fmoc group can be removed using standard basic deprotection conditions.

Q3. What is the optical purity of the product?

The optical purity is ≥99.9% ee. The enzymatic synthesis route supports stereoselective production of the desired L-configured amino acid.

Q4. Can it be used for peptide drug discovery?

Yes. Fmoc-7-methyl-L-tryptophan can be used to prepare modified peptide sequences and analogs for SAR studies, peptide drug discovery, molecular recognition, and stability evaluation. It is particularly useful when researchers want to compare a methylated tryptophan residue with native tryptophan.

Q5. What is the recommended storage condition?

Store tightly sealed at 2–8°C, protected from light and moisture. After opening, minimize exposure to humidity and reseal the container promptly.

Q6. Which solvents can dissolve Fmoc-7-methyl-L-tryptophan?

The product can be dissolved in commonly used organic solvents such as DMF, DCM, and DMSO. For SPPS applications, DMF or DCM can be selected according to the specific synthesis protocol.

Q7. How is the product manufactured?

Hzymes Biotech uses a combined biocatalytic synthesis and chemical protection strategy. Tryptophan synthase catalyzes the formation of 7-methyl-L-tryptophan from 7-methylindole and L-serine, followed by chemical Fmoc protection.

Q8. Is Hzymes Biotech an Fmoc unnatural amino acid supplier?

Hzymes Biotech provides high-purity Fmoc-protected unnatural amino acid building blocks for research and peptide synthesis applications. Product specifications, CoA documentation, packaging, and technical support can be provided according to project requirements.

Q9. Can Hzymes support Fmoc amino acid GMP CDMO projects?

For projects requiring customized synthesis, scale-up, or manufacturing support, Hzymes Biotech can evaluate specific Fmoc amino acid GMP/CDMO requirements based on the target molecule, specifications, scale, and regulatory needs. Please contact the technical or business team for project-specific assessment.