222848-56-8

Upstream product

• 1161-13-3 N-Cbz-L-Phe 
• 150767-05-8 (S)-2-(phenylmethoxycarbonyl)amino-1-phenylbut-3-ene 
• 200616-24-6 (3S)-N-(benzyloxycarbonyl)-3-amino-4-phenylbutane-1,2-diol 
• 6372-14-1 N-((benzyloxy)carbonyl)-L-phenylalaninol 
• 59830-60-3 benzyl (1S)-(1-formyl-2-phenylethyl)carbamate 
• 243842-83-3 (2RS,3S)-3-(benzyloxycarbonyl)amino-2-hydroxy-4-phenylbutanenitrile 

Downstream Products

• 227317-36-4 [(S)-1-Benzyl-3-((S)-2-tert-butylcarbamoyl-pyrrolidin-1-yl)-2-hydroxy-3-oxo-propyl]-carbamic acid benzyl ester 
• 141197-75-3 (3S)-3-(N-benzyloxycarbonyl)amino-2-keto-4-phenylbutyryl-L-prolyl-tert-butyl amide 
• 191849-91-9 1-<(2R,3S)-3-benzyloxycarbonylamino-2-hydroxy-4-phenylbutyryl>-N-tert-butyl-L-prolinamide 
• 141171-72-4 (2S,3S)-3-(N-benzyloxycarbonyl)amino-2-hydroxy-4-phenylbutyryl-L-prolyl-tert-butyl amide 

Relevant academic research and scientific papers

Chemoselective catalytic oxidation of 1,2-diols to α-hydroxy acids controlled by TEMPO-ClO2 charge-transfer complex

Chemoselective catalytic oxidation from 1,2-diols to α-hydroxy acids in a cat. TEMPO/cat. NaOCl/NaClO2 system has been achieved. The use of a two-phase condition consisting of hydrophobic toluene and water suppresses the concomitant oxidative cleavage. A study of the mechanism suggests that the observed selectivity is derived from the precise solubility control of diols and hydroxy acids as well as the active species of TEMPO. Although the oxoammonium species TEMPO+Cl- is hydrophilic, the active species dissolves into the organic layer by the formation of the charge-transfer (CT) complex TEMPO-ClO2 under the reaction conditions.

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.