33468-34-7

Usage

Uses

Used in Pharmaceutical Development:
6-Methyl-L-tryptophan is used as a potential therapeutic agent for immune-related disorders, leveraging its ability to inhibit the enzyme IDO. This inhibition can modulate the immune response, making it a candidate for the treatment of conditions such as cancer and inflammatory diseases.
Used in Cancer Treatment:
In the field of oncology, 6-Methyl-L-tryptophan is used as an immunomodulatory agent to enhance the body's natural defenses against cancer. Its ability to inhibit IDO can potentially disrupt tumor growth and progression by altering the immune microenvironment.
Used in Inflammatory Disease Management:
6-Methyl-L-tryptophan is utilized as an anti-inflammatory agent, given its capacity to reduce inflammation through the modulation of immune responses. This makes it a promising candidate for the treatment of various inflammatory conditions.
Used in Neuroprotection:
Due to its neuroprotective properties, 6-Methyl-L-tryptophan is considered for use in neurodegenerative disease research and treatment, potentially offering protection to neurons and supporting brain health.
These applications highlight the multifaceted potential of 6-Methyl-L-tryptophan in the medical and pharmaceutical industries, underscoring the need for further research and development to fully realize its therapeutic potential.

Upstream product

• 187028-77-9 N^α-acetyl-6-methyl-D,L-tryptophan 
• 2280-85-5 6-methyl-DL-tryptophan 
• 3420-02-8 6-methylindole 
• 56-45-1 L-serin 
• 851364-80-2 4-[3-(6-methylindolyl)methyl]-4-hydroxy-2-hydroxyimino-glutalic acid ammonium salt 

Downstream Products

• 1991-93-1 6-methyl-L-tryptophan 
• 67008-97-3 6-methyl-D-tryptophan 

Relevant academic research and scientific papers

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.

Biocatalysts from cyanobacterial hapalindole pathway afford antivirulent isonitriles against MRSA

Abstract: The emergence of resistance to frontline antibiotics has called for novel strategies to combat serious pathogenic infections. Methicillin-resistant Staphylococcus aureus [MRSA] is one such pathogen. As opposed to traditional antibiotics, bacteriostatic anti-virulent agents disarm MRSA, without exerting pressure, that cause resistance. Herein, we employed a thermophilic Thermotoga maritima tryptophan synthase (TmTrpB1) enzyme followed by an isonitrile synthase and Fe(II)-α-ketoglutarate-dependent oxygenase, in sequence as biocatalysts to produce antivirulent indole vinyl isonitriles. We report on conversion of simple derivatives of indoles to their C3-vinyl isonitriles, as the enzymes employed here demonstrated broader substrate tolerance. In toto, eight distinct L-Tryptophan derived α-amino acids (7) were converted to their bioactive vinyl isonitriles (3) by action of an isonitrile synthase (WelI1) and an Fe(II)-α-ketoglutarate-dependent oxygenase (WelI3) yielding structural variants possessing antivirulence against MRSA. These indole vinyl isonitriles at 10 μg/mL are effective as antivirulent compounds against MRSA, as evidenced through analysis of rabbit blood hemolysis assay. Based on a homology modelling exercise, of enzyme-substrate complexes, we deduced potential three dimensional alignments of active sites and glean mechanistic insights into the substrate tolerance of the Fe(II)-α-ketoglutarate-dependent oxygenase. Graphic abstract: [Figure not available: see fulltext.]

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.

COMPOSITIONS AND METHODS FOR CYCLOFRUCTANS AS SEPARATION AGENTS

The present invention relates to derivatized cyclofructan compounds, compositions comprising derivatized cyclofructan compounds, and methods of using compositions comprising derivatized cyclofructan compounds for chromatographic separations of chemical species, including enantiomers. Said compositions may comprise a solid support and/or polymers comprising derivatized cyclofructan compounds.

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.

Amino acid derivatives and sweetening agent

Novel amino acid derivatives (including ones in the form of a salt) such as 2-amino-4-hydroxy-4-ethylcarbamoyl-4-(3-indolylmethyl)butyric acid are provided which can be used as a low-calorie sweetening agent that is excellent in a degree of sweetness, and as an efficient ingredient thereof. These substances can be used as an efficient ingredient of a sweetening agent, and also, can be used for imparting sweetness to products such as beverages and foods requiring sweetness. Therefore, such excellent sweetening agents, and foods or beverages to which sweetness is imparted can be also provided.

Synthesis of tryptophans

The preparation of racemic and optically pure tryptophans is described. The D-enantiomers of the 6-substituted compounds possess a potent sweetening capability. Novel intermediates are also disclosed.