20696-60-0

Usage

Definition

ChEBI: A dipeptide formed from two L-tryptophan residues.

InChI:InChI=1/C22H22N4O3/c23-17(9-13-11-24-18-7-3-1-5-15(13)18)21(27)26-20(22(28)29)10-14-12-25-19-8-4-2-6-16(14)19/h1-8,11-12,17,20,24-25H,9-10,23H2,(H,26,27)(H,28,29)

Upstream product

• 4299-70-1 L-tryptophan methyl ester 
• 73-22-3 L-Tryptophan 

Relevant academic research and scientific papers

Methods of treatment using water-soluble tryptophan-containing peptides obtained by the hydrolysis of hens eggs lysozyme

The present invention relates to a process to produce a composition comprising water-soluble peptides and having a Trp/LNAA ratio of more than 0.15, which comprises hydrolyzing lysozyme, preferably hen eggs lysozyme, to prepare a hydrolysate having a DH of between 5 and 45.

Peptide bond formation by aminolysin-A catalysis: A simple approach to enzymatic synthesis of diverse short oligopeptides and biologically active puromycins

A new S9 family aminopeptidase derived from the actinobacterial thermophile Acidothermus cellulolyticus was cloned and engineered into a transaminopeptidase by site-directed mutagenesis of catalytic Ser491 into Cys. The engineered biocatalyst, designated aminolysin-A, can catalyze the formation of peptide bonds to give linear homo-oligopeptides, hetero-dipeptides, and cyclic dipeptides using cost-effective substrates in a one-pot reaction. Aminolysin-A can recognize several C-terminal-modified amino acids, including the l- and d-forms, as acyl donors as well as free amines, including amino acids and puromycin aminonucleoside, as acyl acceptors. The absence of amino acid esters prevents the formation of peptides; therefore, the reaction mechanism involves aminolysis and not a reverse reaction of hydrolysis. The aminolysin system will be a beneficial tool for the preparation of structurally diverse peptide mimetics by a simple approach.

Synthesis and separation of L-trytophan oligo-peptides assisted by phosphorus oxychloride

With the assistance of inorganic phosphorus, α-amino acids could self-assemble into a series of oligopeptides, so it could provide a new route to synthesize peptides. In this paper, the self-assembly reaction of L-trytophan mediated by phosphorus oxychloride was monitored by using ESI-MS. The proper condition of the self-assembly reaction of L-Try was reported. The reaction products were purified by RP-HPLC and the fragmentation pathway for L-Try oligo-peptides were analyzed by using ESI-MS/MS.