496929-99-8

Usage

Uses

Used in Pharmaceutical Industry:
7-Bromo-D-tryptophan is used as a building block for the synthesis of bioactive compounds, specifically for the development of antimicrobial and anticancer agents. Its unique structure allows for the creation of novel therapeutics with enhanced efficacy and selectivity.
Used in Biochemical and Biophysical Research:
7-Bromo-D-tryptophan serves as a valuable tool in biochemical and biophysical research, enabling scientists to study the interactions and mechanisms of various biological processes. Its chiral nature provides insights into the role of stereochemistry in molecular recognition and function.
Used in Biosynthesis of Natural Products:
7-Bromo-D-tryptophan has been investigated for its role in the biosynthesis of natural products in certain organisms. Understanding its involvement in these processes can lead to the discovery of new bioactive compounds and enhance our knowledge of metabolic pathways.

Upstream product

• 75816-18-1 N-acetyl-7'-bromo-DL-tryptophan 
• 496929-98-7 N-acetyl-7'-bromo-D-tryptophan 
• 2861-59-8 N-formylindoline 
• 577-19-5 2-nitrophenyl bromide 
• 153-94-6 D-tryptophan 
• 852391-45-8 DL-7-Bromo-tryptophan 
• 62813-85-8 7-bromo-2,3-dihydroindole 
• 51417-51-7 7-bromo-1H-indole 
• 496-15-1 1-indoline 
• 910808-42-3 7-bromo-N-formylindoline 

Downstream Products

• 496930-00-8 7'-bromo-N-carbobenzyloxy-D-tryptophan 
• 777056-25-4 C₁₂H₁₃BrN₂O₂ 

Relevant academic research and scientific papers

Enzymatic halogenation of tryptophan on a gram scale

Halogenated arenes are important building blocks in medicinal and agrochemistry. Chemical electrophilic aromatic halogenation requires molecular halogen, whereas FADdependent halogenases form halogenated arenes with high regioselectivity while only halide salts and O2 are required. This reaction proceeds at room temperature in aqueous media. However, enzymatic halogenation is considered inefficient, mainly because halogenases are not stable. Thus, the preparative application remained elusive.We were able to show that the long-term stability, hence, the preparative efficiency of the tryptophan-7-halogenase RebH can be significantly improved by immobilization together with the other enzymes required for cofactor regeneration. We established a facile scalable method suitable for the halogenation of tryptophan and its derivatives on a gram scale using a solid, multifunctional, and recyclable biocatalyst; this immobilization strategy might also be applicable for other FAD-dependent halogenases.

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.

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.

General synthesis of unnatural 4-, 5-, 6-, and 7-bromo-D-tryptophans by means of a regioselective indole alkylation

A general two-step approach to enantiopure bromotryptophans from unprotected bromoindoles has been developed. Indole nucleophiles prepared with MeMgCl in the presence of CuCl reacted with cyclic sulfamidates derived from enantiopure D-serine to form 4-, 5-, 6-, or 7-bromo-D-tryptophan and some other halogenated tryptophans in moderate yields but with complete regioselectivity. The bromotryptophan derivatives were deprotected using mild conditions.

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.

Total synthesis guided structure elucidation of (+)-psychotetramine

Solving the puzzles: Total synthesis played a key role in the elucidation of the stereochemistry and verification of the constitution of the complex polymeric natural product psychotetramine. The route features three powerful assembly processes that enabl

Preparation of 7-halo-indoles by thallation of N-formylindoline and their attempted use for synthesis of the right-hand segment of chloropeptin

7-Substituted (Cl, Br, I) indoles were synthesized by using thallation of N-formylindoline as a key reaction. Two precursor tripeptides for the right-hand segment of chloropeptin were synthesized by using (R)-7′-iodo and 7′-bromotryptophans derived from each 7-substituted indole (I, Br) obtained by the above procedure.

Convenient synthesis of 7′ and 6′-bromo-D-tryptophan and their derivatives by enzymatic optical resolution using D-aminoacylase

Compounds 7′ and 6′-bromo-D-tryptophan (1 and 2) which are important derivatives for the synthesis of the chloropeptin and kistamycin A, respectively, were conveniently synthesized by optical resolution from N-acetyl-7′ and 6′-bromo-DL-tryptophan ((RS)-5 and (RS)-14) using D-aminoacylase.