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

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

Uses

Used in Drug Discovery:
6-nitrotryptophan is used as a building block in the production of peptide libraries for drug discovery. Its unique chemical properties allow for the exploration of novel peptide sequences and their interactions with target molecules, facilitating the identification of potential drug candidates.
Used in Protein-Ligand Interaction Studies:
6-nitrotryptophan is utilized as a tool for studying protein-ligand interactions and enzyme kinetics. The presence of the nitro group enables the investigation of binding affinities, specificity, and the influence of the nitro group on the overall protein structure and function.
Used in Fluorescence-Based Protein Dynamics Research:
6-nitrotryptophan has been investigated for its potential use as a fluorescent probe in studying protein dynamics and conformational changes. Its fluorescence properties allow researchers to monitor protein folding, unfolding, and interactions with other molecules in real-time, providing valuable insights into protein behavior and function.
Used in Antimicrobial Applications:
6-nitrotryptophan has been reported to possess antimicrobial properties, making it a promising candidate for the development of new antimicrobial agents. Its ability to target and disrupt microbial processes could lead to the creation of novel treatments for various infectious diseases.
Used in Anticancer Research:
6-nitrotryptophan has also been explored for its potential anticancer properties. Its ability to interact with and modulate cellular processes may offer new avenues for cancer treatment, particularly in the development of targeted therapies that exploit the unique characteristics of cancer cells.

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 
• 116857-21-7 6-nitro-Nα-trifluoroacetyl-L-tryptophan methyl ester 
• 4769-96-4 6-nitroindole 
• 56-45-1 L-serin 
• 73-22-3 L-Tryptophan 

Downstream Products

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

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.

Synthetic studies of cyclic peptides stephanotic acid methyl ester, celogentin C, and moroidin

An account of the total synthesis of stephanotic acid methyl ester and celogentin C is presented. The present synthesis features a tandem asymmetric Michael addition/bromination sequence for the synthesis of leucine-tryptophan moiety, and an oxidative coupling reaction to form the tryptophan-imidazole linkage. Moreover, the total synthesis of moroidin had also been studied, and three different synthetic strategies for the construction of the right-hand ring of moroidin were studied.

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.

Synthesis of the LeuTrp component of the celogentin family of cyclic peptides through a CH activationcross-coupling strategy

A bioinspired approach to the central leucine(C3)-tryptophan(C6) cross-linked moiety present in the celogentin family of cyclic peptide natural products was achieved. The key transformation was enabled through a palladium-catalyzed C-H activationcross-coupling of leucine quinoline amide and 6-iodotryptophan derivatives. X-Ray crystallographic analysis of a β-(indol-6-yl)-leucine derivative confirms the stereochemistry of the cross-linked adduct matches that of the natural products. The method enables the preparation of the Leu-Trp adduct as a single stereoisomer from l-leucine and l-tryptophan.

Regioselective nitration of Nα,N1-bis(trifluoroacetyl)-l-tryptophan methyl ester: Efficient synthesis of 2-nitro and 6-nitro-N-trifluoroacetyl-l-tryptophan methyl ester

Nitration of Nα,N1-bis(trifluoroacetyl)-l-tryptophan methyl ester with HNO3 in acetic anhydride at 0 °C provides Nα-trifluoroacetyl-2-nitro-l-tryptophan methyl ester in 67% yield, whereas nitration in trifluoroacetic acid at 0 °C gives Nα-trifluoroacetyl-6-nitro-l-tryptophan methyl ester in 69% yield.

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.