128053-39-4

Upstream product

• 128018-20-2 N-<1-phenyl-2(S)-<(benzyloxycarbonyl)amino>-3(R)-hydroxybutan>-4-L-prolyl-tert-butyl amide 
• 128018-43-9 N-benzyloxycarbonyl-3(S)-amino-1-chloro-4-phenyl-2(S)-butanol 
• 26049-94-5 (S)-benzyl (4-chloro-3-oxo-1-phenylbutan-2-yl)carbamate 
• 1161-13-3 N-Cbz-L-Phe 
• 128018-18-8 L-proline tert-butylamide 
• 128018-44-0 N-benzyloxycarbonyl-3(S)-amino-1,2(S)epoxy-4-phenylbutane 
• 41518-17-6 Z-Phe-O-COO-isoBu 

Relevant academic research and scientific papers

An unusual functional group interaction and its potential to reproduce steric and electrostatic features of the transition states of peptidolysis

The donor-acceptor interaction between a tertiary amine and an aldehyde, first observed among a select class of alkaloids, was deliberately established in a peptidomimetic (1a-c) to mimic features of the two principal transition states of peptide hydrolys

Development of a new type of protease inhibitors, efficacious against FIV and HIV variants

Based on the structural analysis of FIV protease and drug-resistant HIV proteases and molecular modeling, a new type of inhibitors with a small P3 residue has been developed. These inhibitors are effective against HIV and its drug-resistant mutants, as well as SIV and FIV. Modification of existing HIV protease inhibitors by reducing the size of the P3 residue has the same effect. This finding provides a new strategy for the development of HIV protease inhibitors effective against the wild-type and drug-resistant mutants. It further supports the use of FIV protease as a useful model for drug-resistant HIV proteases, which often have a more constricted binding region for the P3 group or the combined P3 and P1 groups.