118459-71-5

Upstream product

• 186581-53-3 diazomethane 
• 61-90-5 L-leucine 
• 56-86-0 L-glutamic acid 
• 98-88-4 benzoyl chloride 
• 2666-93-5 (S)-Leu-OMe 
• 1466-83-7 N-benzoyl-L-leucine 
• 7517-19-3 methyl (L)-leucinate hydrochloride 
• 25163-98-8 4-isobutyl-2-phenyloxazol-5(4H)-one 
• 65-85-0 benzoic acid 
• 13139-15-6 N-tert-butoxycarbonyl-L-leucine 
• 15136-13-7 N-tert-butoxycarbonyl-L-leucyl-L-leucine methyl ester 

Relevant academic research and scientific papers

Structure-Based Design of Inhibitors Selective for Human Proteasome β2c or β2i Subunits

Subunit-selective proteasome inhibitors are valuable tools to assess the biological and medicinal relevance of individual proteasome active sites. Whereas the inhibitors for the β1c, β1i, β5c, and β5i subunits exploit the differences in the substrate-binding channels identified by X-ray crystallography, compounds selectively targeting β2c or β2i could not yet be rationally designed because of the high structural similarity of these two subunits. Here, we report the development, chemical synthesis, and biological screening of a compound library that led to the identification of the β2c- and β2i-selective compounds LU-002c (4; IC50 β2c: 8 nM, IC50 β2i/β2c: 40-fold) and LU-002i (5; IC50 β2i: 220 nM, IC50 β2c/β2i: 45-fold), respectively. Co-crystal structures with β2 humanized yeast proteasomes visualize protein-ligand interactions crucial for subunit specificity. Altogether, organic syntheses, activity-based protein profiling, yeast mutagenesis, and structural biology allowed us to decipher significant differences of β2 substrate-binding channels and to complete the set of subunit-selective proteasome inhibitors.

The Demonstration of Selective Peptide Bond Formation in Clear Aqueous Solutions

The distribution of dipeptides upon treatment of equimolar amounts of glutamic acid, leucine, and C6H11N=C=N(CH2)3+NMe3-OSO2C6H4Me-p, in clear aqueous solution followed by N,C-protection, was found to be: Bz-Glu(γ-OMe)-Leu-OMe (72percent), Bz-Glu(α-OMe)-Glu-di-OMe (15percent), and Bz-Leu-Leu-OMe (8percent); Bz-Leu-Glu-di-OMe, Bz-Glu(α-OMe)-Leu-OMe, and Bz-Glu(γ-OMe)-Glu-di-OMe could not be detected (Bz = PhCO).

Asymmetric Induction during the Aminolysis of 5(4H)-Oxazolones from N-Benzoyl Amino Acids; Almost Specific Formation of One Epimer in the Reaction of the Oxazolone from N-Benzoyl-DL-t-leucine with Methyl L-Prolinate

Asymmetric induction during the aminolysis of 5(4H)-oxazolones from N-benzoyl amino acids was investigated using a series of amino acid esters as amine nucleophiles.The reaction of the oxazolone from N-benzoyl-DL-t-leucine with methyl L-prolinate was found to produce the diastereomeric D-L isomer, almost specifically, under appropriate conditions.