1416992-34-1

Basic information

• Product Name: benzyl ((S)-3-cyclohexyl-1-oxo-1-(((S)-1-oxo-3-(2-oxopyrrolidin-3-yl)propan-2-yl)amino)propan-2-yl)carbamate
• Synonyms: benzyl ((S)-3-cyclohexyl-1-oxo-1-(((S)-1-oxo-3-(2-oxopyrrolidin-3-yl)propan-2-yl)amino)propan-2-yl)carbamate
• CAS NO: 1416992-34-1
• Molecular Weight: 443.543
• Mol File: 1416992-34-1.mol
• Article Data: 3

Chemical Properties

• CAS DataBase Reference: benzyl ((S)-3-cyclohexyl-1-oxo-1-(((S)-1-oxo-3-(2-oxopyrrolidin-3-yl)propan-2-yl)amino)propan-2-yl)carbamate(CAS DataBase Reference)
• NIST Chemistry Reference: benzyl ((S)-3-cyclohexyl-1-oxo-1-(((S)-1-oxo-3-(2-oxopyrrolidin-3-yl)propan-2-yl)amino)propan-2-yl)carbamate(1416992-34-1)
• EPA Substance Registry System: benzyl ((S)-3-cyclohexyl-1-oxo-1-(((S)-1-oxo-3-(2-oxopyrrolidin-3-yl)propan-2-yl)amino)propan-2-yl)carbamate(1416992-34-1)

Safety Data

• Hazardous Substances Data: 1416992-34-1(Hazardous Substances Data)

Upstream product

• 1385184-01-9 C₈H₁₄N₂O₃*ClH 
• 27527-05-5 L-cyclohexylalanine 
• 40203-89-2 β-cyclohexyl-L-alanine methyl ester isocyanate 
• 1416992-20-5 C₂₅H₃₅N₃O₆ 
• 25341-42-8 (S)-2-benzyloxycarbonylamino-3-cyclohexylpropionic acid 
• 113828-93-6 (S)-2-Benzyloxycarbonylamino-3-cyclohexyl-propionic acid methyl ester 
• 17193-39-4 methyl 3-cyclohexyl-L-alaninate hydrochloride 
• 1416992-27-2 C₂₄H₃₅N₃O₅ 

Downstream Products

• 1416992-42-1 sodium (2S)-2-((S)-2-(((benzyloxy)carbonyl)amino)-3-cyclohexylpropanamido)-1-hydroxy-3-(2-oxopyrrolidin-3-yl)propane-1-sulfonate 
• 1467641-87-7 C₃₈H₄₈N₃O₈P 

Relevant articles and documents

Structure-guided design and optimization of dipeptidyl inhibitors of norovirus 3CL protease. Structure-activity relationships and biochemical, X-ray crystallographic, cell-based, and in vivo studies

Norovirus infection constitutes the primary cause of acute viral gastroenteritis. There are currently no vaccines or norovirus-specific antiviral therapeutics available for the management of norovirus infection. Norovirus 3C-like protease is essential for viral replication, consequently, inhibition of this enzyme is a fruitful avenue of investigation that may lead to the emergence of antinorovirus therapeutics. We describe herein the optimization of dipeptidyl inhibitors of norovirus 3C-like protease using iterative SAR, X-ray crystallographic, and enzyme and cell-based studies. We also demonstrate herein in vivo efficacy of an inhibitor using the murine model of norovirus infection.

Inhibition of norovirus 3CL protease by bisulfite adducts of transition state inhibitors

Noroviruses are the most common cause of acute viral gastroenteritis, accounting for >21 million cases annually in the US alone. Norovirus infections constitute an important health problem for which there are no specific antiviral therapeutics or vaccines. In this study, a series of bisulfite adducts derived from representative transition state inhibitors (dipeptidyl aldehydes and α-ketoamides) was synthesized and shown to exhibit anti-norovirus activity in a cell-based replicon system. The ED 50 of the most effective inhibitor was 60 nM. This study demonstrates for the first time the utilization of bisulfite adducts of transition state inhibitors in the inhibition of norovirus 3C-like protease in vitro and in a cell-based replicon system. The approach described herein can be extended to the synthesis of the bisulfite adducts of other classes of transition state inhibitors of serine and cysteine proteases, such as α-ketoheterocycles and α-ketoesters.