351857-99-3

Basic information

• Product Name: FMOC-5-HYDROXY-DL-TRYPTOPHAN
• Synonyms: FMOC-5-HYDROXY-DL-TRYPTOPHAN;Fmoc-DL-5-Hydroxytryptophan
• CAS NO: 351857-99-3
• Molecular Formula: C26H22N2O5
• Molecular Weight: 442.46
• Mol File: 351857-99-3.mol
• Article Data: 3

Chemical Properties

• Appearance: /
• CAS DataBase Reference: FMOC-5-HYDROXY-DL-TRYPTOPHAN(CAS DataBase Reference)
• NIST Chemistry Reference: FMOC-5-HYDROXY-DL-TRYPTOPHAN(351857-99-3)
• EPA Substance Registry System: FMOC-5-HYDROXY-DL-TRYPTOPHAN(351857-99-3)

Safety Data

• HazardClass: IRRITANT
• Hazardous Substances Data: 351857-99-3(Hazardous Substances Data)

Usage

General Description

FMOC-5-HYDROXY-DL-TRYPTOPHAN is a chemical compound that is commonly used in the field of biochemistry and pharmaceutical research. It is a derivative of the amino acid tryptophan and is often used as a building block in the synthesis of peptides and proteins. FMOC-5-HYDROXY-DL-TRYPTOPHAN is known for its fluorescent properties, which make it useful for studying the structure and function of biomolecules. Additionally, it has been investigated for its potential therapeutic applications, particularly in the treatment of neurological and psychiatric disorders. Overall, FMOC-5-HYDROXY-DL-TRYPTOPHAN plays a crucial role in advancing our understanding of biological processes and has potential implications for the development of new medicines.

Upstream product

• 1953-54-4 indol-5-ol 
• 82911-69-1 N-(9H-fluoren-2-ylmethoxycarbonyloxy)succinimide 
• 4350-09-8 L-5-HTP 
• 28920-43-6 (fluorenylmethoxy)carbonyl chloride 

Relevant articles and documents

Synthesis of redox-active fluorinated 5-hydroxytryptophans as molecular reporters for biological electron transfer

Fluorinated 5-hydroxytryptophans (Fn-5HOWs) were synthesized in gram scale quantities and incorporated into a β-hairpin peptide and the protein azurin. The redox-active Fn-5HOWs exhibit unique radical spectroscopic signatures that expand the function of 5HOW as probes for biological electron transfer.

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.