445306-14-9

Upstream product

• 20430-72-2 7-methoxy-2-phenylquinolin-4-ol 
• 445305-87-3 (2S,4R)-2-((1R,2S)-1-ethoxycarbonyl-2-vinyl-cyclopropylcarbamoyl)-4-(7-methoxy-2-phenyl-quinolin-4-yloxy)-pyrrolidine-1-carboxylic acid tert-butyl ester 
• 259214-70-5 (2S,4R)-4-(7-Methoxy-2-phenyl-quinolin-4-yloxy)-pyrrolidine-1,2-dicarboxylic acid 1-tert-butyl ester 2-methyl ester 
• 259214-37-4 (2S,4R)-1-(tert-butoxycarbonyl)-4-(7-methoxy-2-phenylquinolin-4-yloxy)pyrrolidine-2-carboxylic acid 
• 74844-91-0 1-tert-butyl 2-methyl (2S,4R)-4-hydroxy-1,2-pyrrolidinedicarboxylate 
• 94-02-0 ethyl 3-oxo-3-phenylpropionate 
• 536-90-3 m-Anisidine 

Downstream Products

• 445306-16-1 2(S)-(1(R)-cyclopropanesulfonylamino-carbonyl-2(S)-vinylcyclopropylcarbamoyl)-4(R)-(7-methoxy-2-phenylquinolin-4-yloxy)-pyrrolidine-1-carboxylic acid tert-butyl ester 

Relevant academic research and scientific papers

ALGORITHM FOR DESIGNING IRREVERSIBLE INHIBITORS

The invention is an algorithm and method for designing an inhibitor that covalently binds a target polypeptide. The algorithm and method can be used to rapidly and efficiently convert reversible inhibitors into irreversible inhibitors.

Hepatitis C Virus Inhibitors

Hepatitis C virus inhibitors having the general formula are disclosed. Compositions comprising the compounds and methods for using the compounds to inhibit HCV are also disclosed.

Hepatitis C virus inhibitors

The present disclosure is generally directed to antiviral compounds, and more specifically directed to compounds which inhibit the function of the NS3 protease (also referred to herein as “serine protease”) encoded by Hepatitis C virus (HCV), compositions comprising such compounds, and methods for inhibiting the function of the NS3 protease.

Potent inhibitors of the hepatitis C virus NS3 protease: Design and synthesis of macrocyclic substrate-based β-strand mimics

The virally encoded NS3 protease is essential to the life cycle of the hepatitis C virus (HCV), an important human pathogen causing chronic hepatitis, cirrhosis of the liver, and hepatocellular carcinoma. The design and synthesis of 15-membered ring β-strand mimics which are capable of inhibiting the interactions between the HCV NS3 protease enzyme and its polyprotein substrate will be described. The binding interactions between a macrocyclic ligand and the enzyme were explored by NMR and molecular dynamics, and a model of the ligand/enzyme complex was developed.