128018-20-2

Basic information

• Product Name: N-<1-phenyl-2(S)-<(benzyloxycarbonyl)amino>-3(R)-hydroxybutan>-4-L-prolyl-tert-butyl amide
• Synonyms: N-<1-phenyl-2(S)-<(benzyloxycarbonyl)amino>-3(R)-hydroxybutan>-4-L-prolyl-tert-butyl amide
• CAS NO: 128018-20-2
• Molecular Weight: 467.608
• Mol File: 128018-20-2.mol
• Article Data: 4

Chemical Properties

• CAS DataBase Reference: N-<1-phenyl-2(S)-<(benzyloxycarbonyl)amino>-3(R)-hydroxybutan>-4-L-prolyl-tert-butyl amide(CAS DataBase Reference)
• NIST Chemistry Reference: N-<1-phenyl-2(S)-<(benzyloxycarbonyl)amino>-3(R)-hydroxybutan>-4-L-prolyl-tert-butyl amide(128018-20-2)
• EPA Substance Registry System: N-<1-phenyl-2(S)-<(benzyloxycarbonyl)amino>-3(R)-hydroxybutan>-4-L-prolyl-tert-butyl amide(128018-20-2)

Safety Data

• Hazardous Substances Data: 128018-20-2(Hazardous Substances Data)

Upstream product

• 41518-17-6 Z-Phe-O-COO-isoBu 
• 1161-13-3 N-Cbz-L-Phe 
• 128018-44-0 N-benzyloxycarbonyl-3(S)-amino-1,2(S)epoxy-4-phenylbutane 
• 128018-18-8 L-proline tert-butylamide 
• 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 

Downstream Products

• 128053-39-4 (S)-1-((2R,3S)-3-Amino-2-hydroxy-4-phenyl-butyl)-pyrrolidine-2-carboxylic acid tert-butylamide 

Relevant articles and documents

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.