24587-41-5

Usage

Definition

ChEBI: A dipeptide formed from L-phenylalanine and L-tryptophan residues.

InChI:InChI=1/C20H21N3O3/c21-16(10-13-6-2-1-3-7-13)19(24)23-18(20(25)26)11-14-12-22-17-9-5-4-8-15(14)17/h1-9,12,16,18,22H,10-11,21H2,(H,23,24)(H,25,26)

Upstream product

• 35661-40-6 N-Fmoc L-Phe 
• 143824-78-6 3-[(S)-2-carboxy-2-(9H-fluoren-9-ylmethoxycarbonylamino)ethyl]indole-1-carboxylic acid tert-butyl ester 
• 3081-24-1 H-Phe-OEt 
• 73-22-3 L-Tryptophan 
• 4299-70-1 L-tryptophan methyl ester 
• 83522-39-8 N^α-(tert-butoxycarbonyl)-L-phenylalanyl-L-tryptophan methyl ester 
• 67729-36-6 Boc-Phe-O-COO-isoBu 
• 13734-34-4 N-tert-butoxycarbonyl-L-phenylalanine 
• 83522-40-1 (tert-butoxycarbonyl)-L-phenylalanyl-L-tryptophan 
• 2577-90-4 methyl (2S)-2-amino-3-phenylpropanoate 

Downstream Products

• 77935-23-0 H-Asn-Phe-Phe-Trp-OH 
• 77935-22-9 Z-Asn-Phe-Phe-Trp-OH 

Relevant academic research and scientific papers

γ-Valerolactone (GVL): An eco-friendly anchoring solvent for solid-phase peptide synthesis

Due to the hazardous nature of CH2Cl2, regulatory authorities have imposed restrictions to minimize or even stop its use. It has therefore become imperative to identify environmentally benign solvents to replace it. Here we report on a bio derived solvent, γ-valerolactone, for the incorporation of the first amino acid onto p-alkoxybenzyl alcohol resin in solid-phase peptide synthesis. Satisfactory loading values (by a spectrophotometric method) were achieved. Furthermore, racemization and dipeptide formation were also checked and found to be acceptable.

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.

Engineered transaminopeptidase, aminolysin-S for catalysis of peptide bond formation to give linear and cyclic dipeptides by one-pot reaction

Aminopeptidase from Streptomyces thermocyaneoviolaceus NBRC14271 was engineered into transaminopeptidase and used to catalyze an aminolysis reaction to give linear and cyclic dipeptides from cost-effective substrates such as the ester derivatives of amino