21495-41-0

Usage

Uses

Used in Pharmaceutical Synthesis:
2-METHYL-DL-TRYPTOPHAN is used as a key intermediate in the synthesis of various pharmaceuticals for its ability to contribute to the development of new drugs with potential therapeutic benefits.
Used in Drug Production:
As a starting material, 2-METHYL-DL-TRYPTOPHAN is utilized in the production process of a range of drugs, highlighting its importance in the pharmaceutical industry.
Used in Medical Research:
2-METHYL-DL-TRYPTOPHAN is used as a subject of investigation in medical research for its potential role in treating conditions such as depression and anxiety, given its structural relation to tryptophan, a precursor in the biosynthesis of serotonin.
Used in Organic Chemistry:
In the field of organic chemistry, 2-METHYL-DL-TRYPTOPHAN serves as a valuable precursor in the synthesis of certain natural products, including alkaloids and peptides, contributing to the discovery and development of novel compounds with potential applications.

Upstream product

• 95-20-5 2-methyl-1H-indole 
• 56-45-1 L-serin 
• 37125-92-1 2-methylgramine 
• 64-17-5 ethanol 
• 60587-01-1 N-acetyl-2-methyltryptophan 
• 94437-90-8 acetylamino-(2-methyl-indol-3-ylmethyl)-malonic acid diethyl ester 

Downstream Products

• 5416-80-8 2-methyl-1H-indole-3-carbaldehyde 
• 179764-62-6 4-acetylquinoline-2-carboxylic acid 
• 392-12-1 Indole-3-pyruvic acid 
• 63-91-2 L-phenylalanine 
• 1138220-65-1 3-(2-methylindolyl)pyruvic acid 
• 73-22-3 L-Tryptophan 
• 56-86-0 L-glutamic acid 
• 140852-06-8 (R)-2-amino-3-(2-methyl-1H-indol-3-yl)propanoic acid 

Relevant academic research and scientific papers

Gold-Catalyzed Spirocyclization Reactions of N-Propargyl Tryptamines and Tryptophans in Aqueous Media

N-Propargyl tryptamine and tryptophan derivatives that are readily available from both synthetic and biocatalytic approaches undergo gold-catalyzed dearomative cyclizations in aqueous media to the corresponding spirocyclic derivatives. In addition to the efficiency of the method, operating in aqueous media affords a selective entry to C2-unsubstituted spiroindolenines that have long remained unattainable by Au(I) catalysis. Moderate to excellent yields of the desired spirocyclic products bearing various substituents were obtained.

Dynamic Kinetic Resolution for Asymmetric Synthesis of L-Noncanonical Amino Acids from D-Ser Using Tryptophan Synthase and Alanine Racemase

L-Ser is often used to synthesize some significant l-noncanonical α-amino acids(l-ncAAs), which are the prevalent intermediates and precursors for functional synthetic compounds. In this study, threonine aldolase from Escherichia coli k-12 MG1655 has been used to synthesize l-Ser. In contrast to the maximum catalytic capacity (20 g/L) for l-threonine aldolase(LTA), d-Ser was synthesized with high yield (240 g/L) from cheap Gly and paraformaldehyde using d-threonine aldolase (DTA) from Arthrobacter sp ATCC. In order to fully utilize d-Ser and expand the resource of l-Ser, a dynamic kinetic resolution system was constructed to convert d/dl-Ser to l-Ser through combining alanine racemase (Alr) from Bacillus subtilis with l-tryptophan synthase (TrpS) from Escherichia coli k-12 MG1655, and l-ncAAs including l-Trp and l-Cys derivatives were synthesized with excellent enantioselectivity and in high yields. The results indicated l-ncAAs could be efficiently synthesized from d-Ser using this original and green dynamic kinetic resolution system, and the reliable l-Ser resource has been established from simple and achiral substrates.

Processing 2-Methyl- l -Tryptophan through Tandem Transamination and Selective Oxygenation Initiates Indole Ring Expansion in the Biosynthesis of Thiostrepton

Thiostrepton (TSR), an archetypal member of the family of ribosomally synthesized and post-translationally modified thiopeptide antibiotics, possesses a biologically important quinaldic acid (QA) moiety within the side-ring system of its characteristic thiopeptide framework. QA is derived from an independent l-Trp residue; however, its associated transformation process remains poorly understood. We here report that during the formation of QA, the key expansion of an indole to a quinoline relies on the activities of the pyridoxal-5′-phosphate-dependent protein TsrA and the flavoprotein TsrE. These proteins act in tandem to process the precursor 2-methyl- l-Trp through reversible transamination and selective oxygenation, thereby initiating a highly reactive rearrangement in which selective C2-N1 bond cleavage via hydrolysis for indole ring-opening is closely coupled with C2′-N1 bond formation via condensation for recyclization and ring expansion in the production of a quinoline ketone intermediate. This indole ring-expansion mechanism is unusual, and represents a new strategy found in nature for l-Trp-based functionalization.

OLIGOPEPTIDE COMPOUNDS CONTAINING D-2-ALKYLTRYPTOPHAN CAPABLE OF PROMOTING THE RELEASE OF GROWTH HORMONE

A peptide of formula: A-D-X-D-Mrp-B wherein A is hydrogen, 2-aminoisobutyryl, 4-aminobutyryl, D relates to the dextro isomer, X is Mrp, wherein Mrp means 2-alkyltryptophan or X is a residue of protected serine, Ser (Y), wherein Y can be benzyl, p-chlorobenzyl, 4-methoxybenzyl, 2,4,6-trimethoxybenzyl, tert-butyl; B is NR2R3, wherein R2 and R3, which can be the same or different, are hydrogen or a C1-C3 alkyl group; an OR4 group, wherein R4 is hydrogen or a C1-C3 alkyl C-Lys-NH2 group, wherein C is Phe or Mrp, and the addition salts with pharmaceutically acceptable organic or inorganic acids of anyone of said polipeptides; these compounds are capable of promoting the release of growth hormone and they are active by the oral route.

Peptides containing D-2-Alkyl-Tryptophan

Peptides containing in its amino acid chain a D-2-alkylTryptophan residue wherein the alkyl group has between one and three carbon atoms and having pharmacological activity equal to or greater than that of analogous peptides containing natural unsubstituted D-Tryptophan residues in place of the D-2-alkylTryptophan. These peptides are more resistant to oxidative degradation which usually takes place, for example, in the presence of reactive radicals or during high energy sterilization than unsubstituted Tryptophan containing peptides.

Fluorescence Studies with Tryptophan Analogues: Excited State Interactions Involving the Side Chain Amino Group

The fluorescence of a large set of tryptophan analogues, including several that are conformationally constrained, was studied.The constrained analogues include tetrahydrocarboline-3-carboxylic acid and 3-amino-3-carboxytetrahydrocarbazole.Steady state and time-resolved fluorescence measurements were made as a function of pH.The fluorescence quantum yields of the constrained analogues are higher than those for the unconstrained counterparts.The emission intensity of the constrained analogues, as well as 4-methyltryptophan, decreases with deprotonation of the side chain α-ammonium groups; this is in contrast to the increase in fluorescence of tryptophan with deprotonation of this group.These results are consistent with the existence of excited state proton transfer to carbon 4 of the indole ring as a quenching mechanism, which is sterically prohibited in the constrained analogues and 4-methyltryptophan.From quantum yield and lifetime data (most decays are nonexponential), the effective rate constant for nonradiative depopulation of the excited state was calculated.For tryptophan analogues having two side chain functional groups, there is a synergistic effect; the presence of two side chain groups causes more quenching than expected from the sum of the individual contributions.For analogues having an α-ammonium group, this synergism appears to be correlated with an induced change in the pKa of this group.Deprotonation of this α-ammonium group also caused a red shift in the emission of these compounds; this appears to be due to electrostatic repulsion between the α-NH3+ group and the excited indole dipole.