831210-89-0

Basic information

• Product Name: Fmoc-L-kynurenine
• Synonyms: Fmoc-L-kynurenine
• CAS NO: 831210-89-0
• Molecular Weight: 430.46
• Mol File: 831210-89-0.mol
• Article Data: 1

Chemical Properties

• Boiling Point: 723.5±60.0 °C(Predicted)
• Density: 1.341±0.06 g/cm3(Predicted)
• CAS DataBase Reference: Fmoc-L-kynurenine(CAS DataBase Reference)
• NIST Chemistry Reference: Fmoc-L-kynurenine(831210-89-0)
• EPA Substance Registry System: Fmoc-L-kynurenine(831210-89-0)

Safety Data

• Hazardous Substances Data: 831210-89-0(Hazardous Substances Data)

Usage

General Description

Fmoc-L-kynurenine is a chemical compound used in the field of biochemistry and organic chemistry. It is a derivative of the amino acid L-tryptophan and is commonly used in the synthesis of peptides and proteins. Fmoc-L-kynurenine is often employed as a building block in solid-phase peptide synthesis, where it serves as a reactive group for the attachment of other amino acids and peptide chains. The Fmoc (Fluorenylmethyloxycarbonyl) group is a protecting group that helps to prevent unwanted reactions during the synthesis process. Overall, Fmoc-L-kynurenine is a valuable tool for the production of synthetic peptides and has applications in both research and industrial settings.

Upstream product

• 1290040-15-1 Fmoc-NFK 
• 2922-83-0 L-kynurenine 
• 3978-11-8 (S )-2-Amino-4-(2-formamidophenyl)-4-oxobutanoic acid 
• 73-22-3 L-Tryptophan 
• 236094-74-9 2-amino-3-(2-oxoindolin-3-yl)propanoic acid 

Relevant articles and documents

Synthesis of peptides containing 5-hydroxytryptophan, oxindolylalanine, N-formylkynurenine and kynurenine

ROS, continuously produced in cells, can reversibly or irreversibly oxidize proteins, lipids, and DNA. At the protein level, cysteine, methionine, tryptophan, and tyrosine residues are particularly prone to oxidation. Here, we describe the solid phase synthesis of peptides containing four different oxidation products of tryptophan residues that can be formed by oxidation in proteins in vitro and in vivo: 5-HTP, Oia, Kyn, and NFK. First, we synthesized Oia and NFK by selective oxidation of tryptophan and then protected the ${bf alpha}$-amino group of both amino acids, and the commercially available 5-HTP, with Fmoc-succinimide. High yields of Fmoc-Kyn were obtained by acid hydrolysis of Fmoc-NFK. All four Fmoc derivatives were successfully incorporated, at high yields, into three different peptide sequences from skeletal muscle actin, creatin kinase (M-type), and ${bf beta}$-enolase. The correct structure of all modified peptides was confirmed by tandem mass spectrometry. Interestingly, isobaric peptides containing 5-HTP and Oia were always well separated in an acetonitrile gradient with TFA as the ion-pair reagent on a C18-phase. Such synthetic peptides should prove useful in future studies to distinguish isobaric oxidation products of tryptophan.