17808-35-4

Basic information

• Product Name: 6-chlorotryptophan
• Synonyms: 6-chlorotryptophan;Tryptophan, 6-chloro-
• CAS NO: 17808-35-4
• Molecular Formula: C11H11 Cl N2 O2
• Molecular Weight: 0
• Mol File: 17808-35-4.mol
• Article Data: 29

Chemical Properties

• Boiling Point: 476.9°Cat760mmHg
• Flash Point: 242.2°C
• Appearance: /
• Density: 1.474g/cm³
• CAS DataBase Reference: 6-chlorotryptophan(CAS DataBase Reference)
• NIST Chemistry Reference: 6-chlorotryptophan(17808-35-4)
• EPA Substance Registry System: 6-chlorotryptophan(17808-35-4)

Safety Data

• Hazardous Substances Data: 17808-35-4(Hazardous Substances Data)

Usage

General Description

6-chlorotryptophan is a modified form of the amino acid tryptophan in which a chlorine atom has been substituted for a hydrogen atom at the sixth position on the tryptophan molecule. This chemical modification can be used to alter the properties and functions of proteins and peptides that contain tryptophan, including enzymes and structural proteins. 6-chlorotryptophan has been studied for its potential applications in pharmaceuticals, as well as in probing the structure and function of proteins in biological systems. It has been found to modulate protein-protein interactions and enzymatic activities, making it a valuable tool in research and drug development. However, further studies are needed to fully understand its potential uses and effects in various biological systems.

InChI:InChI=1/C11H11ClN2O2/c12-7-1-2-8-6(3-9(13)11(15)16)5-14-10(8)4-7/h1-2,4-5,9,14H,3,13H2,(H,15,16)

Upstream product

• 57233-85-9 N-Formyl-6-chlortryptophan 
• 56777-76-5 N^α-acetyl-6-chloro-D-tryptophan 
• 73-22-3 L-Tryptophan 
• 50517-10-7 N^α-acetyl-6-chloro-D,L-tryptophan 
• 17422-33-2 6-chloroindole 
• 56-45-1 L-serin 
• 808145-70-2 6-Chloro-3-((2S,5R)-3,6-diethoxy-5-isopropyl-2,5-dihydro-pyrazin-2-ylmethyl)-2-triethylsilanyl-1H-indole 
• 220906-11-6 (2R,5S)-3,6-diethoxy-2-isopropyl-5-[3-(triethylsilyl)prop-2-ynyl]-2,5-dihydropyrazine 
• 89-63-4 4-Chloro-2-nitroaniline 
• 6828-35-9 5-chloro-2-iodoaniline 
• 5446-05-9 4-chloro-2-nitroiodobenzene 
• 769973-15-1 (3S,6R)-3-[[1-(tert-butyloxycarbonyl)-6-chloro-3-indolyl]methyl]-3,6-dihydro-6-isopropyl-2,5-diethoxypyrazine 
• 1027297-43-3 tert-butyl 3-(bromomethyl)-6-chloro-1H-indole-1-carboxylate 
• 441801-02-1 ethyl 6-chloro-3-methyl-1H-indole-2-carboxylate 

Downstream Products

• 175777-22-7 L-4-chlorokynurenine 
• 56632-86-1 D-6-chlorotryptophan 
• 1219168-45-2 Fmoc-D-6Cl-Trp 
• 3670-19-7 2-(6-chloro-1H-indole-3-yl)ethan-1-amine 
• 1217738-82-3 (S)-N-boc-6-chloro-tryptophan 

Relevant articles and documents

Synthesis of L-6-chloropyrroloindoline of chloptosin cyclohexapeptide

Chloptosin is an apoptosis-inducing dimeric cyclohexapeptide. Enantio-selective synthesis of L-6-chloropyrroloindoline, as the key chiral synthon of the cyclohexapeptide of chloptosin, was successfully achieved starting from 3-chloroaniline by utilizing F

Structure and biocatalytic scope of thermophilic flavin-dependent halogenase and flavin reductase enzymes

Flavin-dependent halogenase (Fl-Hal) enzymes have been shown to halogenate a range of synthetic as well as natural aromatic compounds. The exquisite regioselectively of Fl-Hal enzymes can provide halogenated building blocks which are inaccessible using standard halogenation chemistries. Consequently, Fl-Hal are potentially useful biocatalysts for the chemoenzymatic synthesis of pharmaceuticals and other valuable products, which are derived from haloaromatic precursors. However, the application of Fl-Hal enzymes, in vitro, has been hampered by their poor catalytic activity and lack of stability. To overcome these issues, we identified a thermophilic tryptophan halogenase (Th-Hal), which has significantly improved catalytic activity and stability, compared with other Fl-Hal characterised to date. When used in combination with a thermostable flavin reductase, Th-Hal can efficiently halogenate a number of aromatic substrates. X-ray crystal structures of Th-Hal, and the reductase partner (Th-Fre), provide insights into the factors that contribute to enzyme stability, which could guide the discovery and engineering of more robust and productive halogenase biocatalysts.

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.

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.