831210-89-0 Usage
Uses
Used in Pharmaceutical and Biochemical Research:
Fmoc-L-kynurenine is used as a synthetic building block for the creation of peptides and proteins. Its role in solid-phase peptide synthesis is crucial, as it allows for the stepwise addition of other amino acids and peptide chains, facilitating the development of complex peptide structures.
Used in Organic Chemistry:
In the realm of organic chemistry, Fmoc-L-kynurenine is utilized as a reagent and intermediate in various chemical reactions. Its unique structure and the presence of the Fmoc protecting group make it a versatile component in the synthesis of a wide range of organic compounds.
Used in Industrial Production:
Fmoc-L-kynurenine is employed as a key component in the industrial manufacturing of synthetic peptides and proteins. Its use in this context ensures the efficient and controlled production of these biologically active molecules, which are essential in various industries such as pharmaceuticals, cosmetics, and agriculture.
Overall, Fmoc-L-kynurenine's applications are diverse, highlighting its importance in the synthesis of peptides and proteins, and its utility across different sectors, from research to industrial production.
Check Digit Verification of cas no
The CAS Registry Mumber 831210-89-0 includes 9 digits separated into 3 groups by hyphens. The first part of the number,starting from the left, has 6 digits, 8,3,1,2,1 and 0 respectively; the second part has 2 digits, 8 and 9 respectively.
Calculate Digit Verification of CAS Registry Number 831210-89:
(8*8)+(7*3)+(6*1)+(5*2)+(4*1)+(3*0)+(2*8)+(1*9)=130
130 % 10 = 0
So 831210-89-0 is a valid CAS Registry Number.
831210-89-0Relevant academic research and scientific papers
Synthesis of peptides containing 5-hydroxytryptophan, oxindolylalanine, N-formylkynurenine and kynurenine
Todorovski, Toni,Fedorova, Maria,Hennig, Lothar,Hoffmann, Ralf
, p. 256 - 262 (2012/01/13)
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.
