1416992-42-1

Basic information

• Product Name: sodium (2S)-2-((S)-2-(((benzyloxy)carbonyl)amino)-3-cyclohexylpropanamido)-1-hydroxy-3-(2-oxopyrrolidin-3-yl)propane-1-sulfonate
• Synonyms: sodium (2S)-2-((S)-2-(((benzyloxy)carbonyl)amino)-3-cyclohexylpropanamido)-1-hydroxy-3-(2-oxopyrrolidin-3-yl)propane-1-sulfonate
• CAS NO: 1416992-42-1
• Molecular Weight: 547.605
• Mol File: 1416992-42-1.mol
• Article Data: 2

Chemical Properties

• CAS DataBase Reference: sodium (2S)-2-((S)-2-(((benzyloxy)carbonyl)amino)-3-cyclohexylpropanamido)-1-hydroxy-3-(2-oxopyrrolidin-3-yl)propane-1-sulfonate(CAS DataBase Reference)
• NIST Chemistry Reference: sodium (2S)-2-((S)-2-(((benzyloxy)carbonyl)amino)-3-cyclohexylpropanamido)-1-hydroxy-3-(2-oxopyrrolidin-3-yl)propane-1-sulfonate(1416992-42-1)
• EPA Substance Registry System: sodium (2S)-2-((S)-2-(((benzyloxy)carbonyl)amino)-3-cyclohexylpropanamido)-1-hydroxy-3-(2-oxopyrrolidin-3-yl)propane-1-sulfonate(1416992-42-1)

Safety Data

• Hazardous Substances Data: 1416992-42-1(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 
• 1416992-34-1 benzyl ((S)-3-cyclohexyl-1-oxo-1-(((S)-1-oxo-3-(2-oxopyrrolidin-3-yl)propan-2-yl)amino)propan-2-yl)carbamate 
• 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 

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.