138514-97-3

Usage

Uses

Used in Scientific Research:
7-Fluoro-L-tryptophan is used as a research compound for studying protein-protein interactions, protein structure and dynamics, and biological processes in the fields of biochemistry, immunology, and neuroscience. The fluorination of tryptophan provides unique chemical properties that can be advantageous in these research contexts.
Used in Biochemistry:
7-Fluoro-L-tryptophan is used as a modified amino acid to investigate the effects of fluorination on protein structure and function, as well as to explore the potential applications of fluorinated amino acids in the development of new bioactive molecules.
Used in Immunology:
7-Fluoro-L-tryptophan is used as a tool to study the role of tryptophan in immune system processes and to understand how the fluorination of tryptophan may influence immune responses and interactions.
Used in Neuroscience:
7-Fluoro-L-tryptophan is used as a research compound to explore the role of tryptophan in neural function and to investigate the effects of fluorination on neurotransmitter synthesis and signaling pathways in the nervous system.

Upstream product

• 387-44-0 7-fluoro-1H-indole 
• 56-45-1 L-serin 

Downstream Products

• 1956434-65-3 Fmoc-D-7F-Trp 

Relevant academic research and scientific papers

Dimethylallyltryptophan synthase. An enzyme-catalyzed electrophilic aromatic substitution

Dimethylallyltryptophan (DMAT) synthase catalyzes the alkylation of L-tryptophan at C(4) by dimethylallyl diphosphate (DMAPP) in the first pathway-specific step in the biosynthesis of ergot alkaloids. The mechanism of the reaction was studied with analogs of both substrates. Five 7-substituted derivatives of N-acetyltryptophan (2, Z = OCH3, CH3, F, CF3, and NO2) were synthesized. The L enantiomers of the free amino acids were obtained by selective hydrolysis of the racemate using aminoacylase from Aspergillus. In addition, the E and Z fluoromethyl and difluoromethyl analogs of DMAPP (1, Y = CH3, CH2F, CHF2) were prepared. Rates of the enzyme-catalyzed reactions were measured for the dimethylallyl derivatives with L-tryptophan and for the L-tryptophan derivatives with DMAPP. In addition, the relative reactivities of the methanesulfonate derivatives of the DMAPP analogs were determined for solvolysis in aqueous acetone. A Hammett plot for the tryptophan analogs gave a good linear correlation with p = -2.0. In addition, a Hammett plot of the logarithms of the relative rates of solvolysis and enzyme-catalyzed alkylation gave a positive linear correlation. These results indicate that the prenyl-transfer reaction catalyzed by DMAT synthase is an electrophilic aromatic substitution and is mechanistically similar to the electrophilic alkylation catalyzed by farnesyl diphosphate synthase.

Tuning the Biological Activity of RGD Peptides with Halotryptophans ?

An array of l- and d-halotryptophans with different substituents at the indole moiety was synthesized employing either enzymatic halogenation by halogenases or incorporation of haloindoles using tryptophan synthase. Introduction of these Trp derivatives into RGD peptides as a benchmark system was performed to investigate their influence on bioactivity. Halotryptophan-containing RGD peptides display increased affinity toward integrin αvβ3 and enhanced selectivity over integrin α5β1. In addition, bromotryptophan was exploited as a platform for late-stage diversification by Suzuki-Miyaura cross-coupling (SMC), resulting in new-to-nature biaryl motifs. These peptides show enhanced affinity toward αvβ3, good affinity to αvβ8, and remarkable selectivity over α5β1 and αIIbβ3 while featuring fluorogenic properties. Their feasibility as a probe was demonstrated in vitro. Extensive molecular dynamics simulations were undertaken to elucidate NMR and high-performance liquid chromatography (HPLC) data for these late-stage diversified cyclic RGD peptides and to further characterize their conformational preferences.