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
• Article Data: 8

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

General Description

6-bromo-D-tryptophan is a chemical compound belonging to the class of chemical entities called bromobenzenes. Bromobenzenes are compounds containing a monocyclic benzene moiety that carries one or more bromine atoms. Specifically, 6-bromo-D-tryptophan is a tryptophan derivative, essentially composed of a tryptophan molecule that is substituted by a bromine atom at the 6-position. Tryptophan is a standard amino acid that is found in most proteins. The 'D' in 6-bromo-D-tryptophan signifies that it is a D-isomer, a term relating to its stereochemistry or spatial arrangement of its atoms. 6-broMo-D-tryptophan does not have significant industrial use, but it may be used in scientific research, specifically in the study of proteins.

Upstream product

• 52415-29-9 6-bromo-1H-indole 
• 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 
• 60956-26-5 4-bromo-2-nitrotoluene 

Downstream Products

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

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.

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.