496930-10-0

Basic information

• Product Name: 6-broMo-D-tryptophan
• Synonyms: 6-broMo-D-tryptophan;(R)-2-Amino-3-(6-bromo-1H-indol-3-yl)propanoic acid;D-Tryptophan, 6-bromo-;D-6-Bromotryptophan
• CAS NO: 496930-10-0
• Molecular Formula: C₁₁H₁₁BrN₂O₂
• Molecular Weight: 283.12124
• EINECS: -0
• Mol File: 496930-10-0.mol

Chemical Properties

• Appearance: /
• Storage Temp.: 2-8°C
• CAS DataBase Reference: 6-broMo-D-tryptophan(CAS DataBase Reference)
• NIST Chemistry Reference: 6-broMo-D-tryptophan(496930-10-0)
• EPA Substance Registry System: 6-broMo-D-tryptophan(496930-10-0)

Safety Data

• Hazardous Substances Data: 496930-10-0(Hazardous Substances Data)

Usage

Uses

Used in Scientific Research:
6-bromo-D-tryptophan is used as a research compound for studying proteins. Its unique structure allows researchers to investigate the effects of bromination on the properties and functions of proteins, which can provide insights into various biological processes and potential applications in drug development and understanding protein interactions.

Upstream product

• 85515-06-6 N^α-acetyl-6-bromo-D,L-tryptophan 
• 153-94-6 D-tryptophan 
• 33599-61-0 6-bromo-tryptophan(Ref_.7.) 
• 99474-21-2 (E)-2-(4-bromo-2-nitrophenyl)-N,N-dimethylethyleneamine 
• 52415-29-9 6-bromo-1H-indole 
• 60956-26-5 4-bromo-2-nitrotoluene 

Downstream Products

• 496930-12-2 6'-bromo-N-carbobenzyloxy-D-tryptophan 
• 774181-71-4 C₁₂H₁₃BrN₂O₂ 
• 753504-16-4 Fmoc-D-6Br-Trp 

Relevant articles and documents

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.

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.

Targeted Enzyme Engineering Unveiled Unexpected Patterns of Halogenase Stabilization

Halogenases are valuable biocatalysts for selective C?H activation, but despite recent efforts to broaden their application scope by means of protein engineering, improvement of thermostability and catalytic efficiency is still desired. A directed evoluti

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.

Biosynthesis of l-4-Chlorokynurenine, an Antidepressant Prodrug and a Non-Proteinogenic Amino Acid Found in Lipopeptide Antibiotics

l-4-Chlorokynurenine (l-4-Cl-Kyn) is a neuropharmaceutical drug candidate that is in development for the treatment of major depressive disorder. Recently, this amino acid was naturally found as a residue in the lipopeptide antibiotic taromycin. Herein, we report the unprecedented conversion of l-tryptophan into l-4-Cl-Kyn catalyzed by four enzymes in the taromycin biosynthetic pathway from the marine bacterium Saccharomonospora sp. CNQ-490. We used genetic, biochemical, structural, and analytical techniques to establish l-4-Cl-Kyn biosynthesis, which is initiated by the flavin-dependent tryptophan chlorinase Tar14 and its flavin reductase partner Tar15. This work revealed the first tryptophan 2,3-dioxygenase (Tar13) and kynurenine formamidase (Tar16) enzymes that are selective for chlorinated substrates. The substrate scope of Tar13, Tar14, and Tar16 was examined and revealed intriguing promiscuity, thereby opening doors for the targeted engineering of these enzymes as useful biocatalysts.

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.

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.

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.