154092-61-2

Upstream product

• 62965-35-9 N-tert-butyloxycarbonyl-L-tert-leucine 
• 100-51-6 benzyl alcohol 
• 100-39-0 benzyl bromide 
• 20859-02-3 L-tert-Leucine 
• 24424-99-5 di-tert-butyl dicarbonate 

Downstream Products

• 453509-76-7 N¹-(2-benzylcarbamoyl-2-hydroxy-1-methyl-ethyl)-2-[2-(3,3-dimethyl-butyrylamino)-3,3-dimethyl-butyrylamino]-N⁴,N⁴-dimethyl-succinamide 
• 572924-87-9 N-(phenoxycarbonyl)-L-tert-leucine benzyl ester 
• 1035377-62-8 (S)-benzyl 2-(3-(cyclopropylmethyl)ureido)-3,3-dimethylbutanoate 
• 2243773-95-5 benzyl (S)-2-((S)-2-((tert-butoxycarbonyl)amino)-3,3-dimethylbutanamido)-3,3-dimethylbutanoate 
• 864801-58-1 C₁₄H₁₇NO₃ 
• 1363151-14-7 tert-butyl (S)-1-((S)-1-((S)-2-(4-(3-chloro-2,4-difluorophenylamino)-7-methoxyquinazolin-6-ylcarbamoyl)azetidine-1-yl)-3,3-dimethyl-1-oxobutan-2-ylamino)-1-oxopropan-2-yl(methyl)carbamate 
• 1363150-32-6 (S)-benzyl 2-((S)-2-(tert-butoxycarbonyl(methyl)amino)propanamido)-3,3-dimethylbutanoate 

Relevant academic research and scientific papers

P3-P4 ureas and reverse carbamates as potent HCV NS3 protease inhibitors: Effective transposition of the P4 hydrogen bond donor

A series of tripeptidic acylsulfonamide inhibitors of HCV NS3 protease were prepared that explored structure-activity relationships (SARs) at the P4 position, and their in vitro and in vivo properties were evaluated. Enhanced potency was observed in a ser

QUINOLINE OR QUINAZOLINE DERIVATIVES WITH APOPTOSIS INDUCING ACTIVITY ON CELLS

Provided is a pharmaceutical composition comprising, as an active ingredient, a quinoline or quinazoline derivative of formula (I), a pharmaceutically acceptable salt, an isomer, a hydrate, and a solvate thereof, which is effective in the prevention and treatment of a cancer, inflammation, autoimmune diseases or neurodegenerative disorders which are induced by the overexpression of inhibitor of apoptosis proteins (IAPs).

Toward the back-up of Boceprevir (SCH 503034): Discovery of new extended P4-capped ketoamide inhibitors of hepatitis C virus NS3 serine protease with improved potency and pharmacokinetic profiles

Hepatitis C is the most prevalent liver disease. Viral hepatitis C (HCV), a small (+)-RNA virus, infects chronically an estimated 300 million people worldwide. Results of Phase I clinical studies with our first generation HCV inhibitor Boceprevir, SCH 503034 (1), presented at the 56th Annual Meeting of the American Association for the Study of Liver Diseases (AASLD) were encouraging, and thus, additional human clinical studies are underway. In view of the positive data from our first generation compound, further work aimed at optimizing its overall profile was undertaken. Herein, we report that extension of our earlier inhibitor to the P4 pocket and optimization of the P1′ capping led to the discovery of new ketoamide inhibitors of the HCV NS3 serine protease with improved in vitro potency. In addition to being potent inhibitors of HCV subgenomic RNA replication, some of the new P4-capped inhibitors were also found to have improved PK profile.

HCV INHIBITORS

The present invention is directed to compounds that are antiviral agents. Specifically, the compounds of the present invention inhibit replication of HCV and are therefore useful in treating hepatitis C infections. The present invention is also directed to pharmaceutical compositions comprising these compounds and processes for preparing them.

Substituted cycloalkyl P1' hepatitis C virus inhibitors

The present invention relates to tripeptide compounds, compositions and methods for the treatment of hepatitis C virus (HCV) infection. In particular, the present invention provides novel tripeptide analogs, pharmaceutical compositions containing such analogs and methods for using these analogs in the treatment of HCV infection.

HEPATITIS C INHIBITOR COMPOUNDS

Compounds of formula (I): wherein B, X, R3, L0, L1, L2, R2, R1 and RC are defined herein. The compounds are useful as inhibitors of HCV NS3 protease for the treatment of hepatitis C viral infection.

Short synthesis of protease inhibitors via modified Passerini condensation of N-Boc-α-aminoaldehydes

Extension of the previously reported modification of Passerini multicomponent reaction (involving condensation with N-Boc-α-aminoaldehydes followed by a deprotection-transacylation step) to α-aminoacid derived carboxylic or isocyanide components, allowed the highly convergent and short synthesis of complex peptidomimetic structures, including known potent inhibitors of serine proteases.