1333231-44-9

Upstream product

• 1350624-45-1 C₁₃H₂₂N₂O₅ 
• 1350624-48-4 C₂₂H₃₁N₃O₆ 
• 1333231-43-8 C₂₁H₃₁N₃O₅ 
• 61-90-5 L-leucine 
• 30293-88-0 N-carbonyl-L-leucine methyl ester 
• 2018-66-8 Z-Leu-OH 
• 51021-87-5 N-benzyloxycarbonyl-L-leucine methyl ester 
• 7517-19-3 methyl (L)-leucinate hydrochloride 
• 1385184-01-9 C₈H₁₄N₂O₃*ClH 
• 100-51-6 benzyl alcohol 

Downstream Products

• 1333231-50-7 C₂₅H₃₆N₄O₆ 
• 1350624-56-4 C₂₅H₃₈N₄O₆ 
• 1385183-93-6 C₂₄H₃₂N₄O₆ 
• 1385183-94-7 C₂₄H₃₂N₄O₅S 
• 1385183-82-3 benzyl ((S)-1-(((S)-4-(cyclopropylamino)-3,4-dioxo-1-(2-oxopyrrolidin-3-yl)butan-2-yl)amino)-4-methyl-1-oxopentan-2-yl)-carbamate 
• 1385183-73-2 C₂₆H₃₈N₄O₈ 
• 1385183-84-5 C₂₆H₃₆N₄O₈ 
• 1385183-74-3 C₂₈H₄₂N₄O₆ 
• 1416992-39-6 sodium (2S)-2-((S)-2-(((benzyloxy)carbonyl)amino)-4-methylpentanamido)-1-hydroxy-3-(2-oxopyrrolidin-3-yl)propane-1-sulfonate 
• 1385183-69-6 C₂₅H₃₆N₄O₆ 
• 1467641-77-5 C₂₁H₃₂N₃O₈P 
• 1467641-73-1 C₂₅H₄₀N₃O₈P 

Relevant academic research and scientific papers

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.

MACROCYCLIC AND PEPTIDOMIMETIC COMPOUNDS AS BROAD-SPECTRUM ANTIVIRALS AGAINST 3C OR 3C-LIKE PROTEASES OF PICORNAVIRUSES, CALICIVIRUSES AND CORONAVIRUSES

Antiviral protease inhibitors, including macrocylic transition state inhibitors and peptidomimetics are disclosed, along with related antiviral compounds, and methods of using the same to treat or prevent viral infection and disease. The compounds possess broad-spectrum activity against viruses that belong to the picornavirus-like supercluster, which include important human and animal pathogens including noroviruses, sapoviruses, enteroviruses, poliovirus, foot-and-mouth disease virus, hepatitis A virus, human rhinovirus (cause of common cold), human coronavirus (another cause of common cold), transmissible gastroenteritis virus, murine hepatitis virus, feline infectious peritonitis virus, and severe acute respiratory syndrome coronavirus.

Potent inhibition of norovirus by dipeptidyl α-hydroxyphosphonate transition state mimics

The design, synthesis, and evaluation of a series of dipeptidyl α-hydroxyphosphonates is reported. The synthesized compounds displayed high anti-norovirus activity in a cell-based replicon system, as well as high enzyme selectivity.

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.

Potent inhibition of norovirus 3CL protease by peptidyl α-ketoamides and α-ketoheterocycles

Series of structurally-diverse α-ketoamides and α- ketoheterocycles was synthesized and subsequently investigated for inhibitory activity against Norwalk virus 3C protease in vitro, as well as anti-norovirus activity in a cell-based replicon system.

Design, synthesis, and evaluation of inhibitors of Norwalk virus 3C protease

The first series of peptidyl aldehyde inhibitors that incorporate in their structure a glutamine surrogate has been designed and synthesized based on the known substrate specificity of Norwalk virus 3C protease. The inhibitory activity of the compounds wi