46885-76-1

Basic information

• Product Name: 6-nitrotryptophan
• Synonyms: 6-nitrotryptophan;6-Nitro-L-tryptophan
• CAS NO: 46885-76-1
• Molecular Formula: C₁₁H₁₁N₃O₄
• Molecular Weight: 249.22
• Mol File: 46885-76-1.mol
• Article Data: 6

Chemical Properties

• Boiling Point: 534.7°Cat760mmHg
• Flash Point: 277.2°C
• Appearance: /
• Density: 1.541g/cm³
• Vapor Pressure: 2.91E-12mmHg at 25°C
• Refractive Index: 1.726
• CAS DataBase Reference: 6-nitrotryptophan(CAS DataBase Reference)
• NIST Chemistry Reference: 6-nitrotryptophan(46885-76-1)
• EPA Substance Registry System: 6-nitrotryptophan(46885-76-1)

Safety Data

• Hazardous Substances Data: 46885-76-1(Hazardous Substances Data)

Usage

General Description

6-nitrotryptophan is a chemical compound that is synthesized by nitration of the amino acid tryptophan. It is commonly used as a building block in the production of peptide libraries for drug discovery. The presence of the nitro group in the molecule makes it a useful tool for studying protein-ligand interactions and enzyme kinetics. Furthermore, 6-nitrotryptophan has been investigated for its potential use as a fluorescent probe in studying protein dynamics and conformational changes. Additionally, it has been reported to have antimicrobial and anticancer properties, making it a promising candidate for further pharmaceutical research and development.

InChI:InChI=1/C11H11N3O4/c12-9(11(15)16)3-6-5-13-10-4-7(14(17)18)1-2-8(6)10/h1-2,4-5,9,13H,3,12H2,(H,15,16)

Upstream product

• 105902-18-9 N^α-acetyl-6-nitro-D,L-tryptophan 
• 4769-96-4 6-nitroindole 
• 56-45-1 L-serin 
• 73-22-3 L-Tryptophan 
• 116857-21-7 6-nitro-Nα-trifluoroacetyl-L-tryptophan methyl ester 

Downstream Products

• 1208099-22-2 C₄₂H₅₄N₆O₁₁ 
• 1208099-21-1 C₄₂H₅₄BrN₃O₁₁ 
• 112019-35-9 6-nitro-L-tryptophan-phenethyl ester; hydrochloride 

Relevant articles and documents

Unlocking Reactivity of TrpB: A General Biocatalytic Platform for Synthesis of Tryptophan Analogues

Derivatives of the amino acid tryptophan (Trp) serve as precursors for the chemical and biological synthesis of complex molecules with a wide range of biological properties. Trp analogues are also valuable as building blocks for medicinal chemistry and as tools for chemical biology. While the enantioselective synthesis of Trp analogues is often lengthy and requires the use of protecting groups, enzymes have the potential to synthesize such products in fewer steps and with the pristine chemo- and stereoselectivity that is a hallmark of biocatalysis. The enzyme TrpB is especially attractive because it can form Trp analogues directly from serine (Ser) and the corresponding indole analogue. However, many potentially useful substrates, including bulky or electron-deficient indoles, are poorly accepted. We have applied directed evolution to TrpB from Pyrococcus furiosus and Thermotoga maritima to generate a suite of catalysts for the synthesis of previously intractable Trp analogues. For the most challenging substrates, such as nitroindoles, the key to improving activity lay in the mutation of a universally conserved and mechanistically important residue, E104. The new catalysts express at high levels (>200 mg/L of Escherichia coli culture) and can be purified by heat treatment; they can operate up to 75 °C (where solubility is enhanced) and can synthesize enantiopure Trp analogues substituted at the 4-, 5-, 6-, and 7-positions, using Ser and readily available indole analogues as starting materials. Spectroscopic analysis shows that many of the activating mutations suppress the decomposition of the active electrophilic intermediate, an amino-acrylate, which AIDS in unlocking the synthetic potential of TrpB.

Stereocontrolled and efficient total synthesis of (-)-stephanotic acid methyl ester and (-)-celogentin C

(Figure Presented) A highly stereocontrolled and efficient total synthesis of (-)-stephanotlc acid methyl ester and (-)-celogentin C was accomplished In longest linear 14 steps (4.6% overall yield) and In 20 steps (1.6% overall yield) from L-tryptophan, respectively. Highlights of the synthesis include a tandem asymmetric Michael addition/bromination/azidation strategy for a ready access to the leucine-tryptophan moiety (Leu-Trp linkage) and an oxidative coupling reaction to form the indole-imidazole linkage.

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.