1026701-89-2

Basic information

• Product Name: C₂₂H₃₂N₂O₄S
• Synonyms: C₂₂H₃₂N₂O₄S
• CAS NO: 1026701-89-2
• Molecular Weight: 420.573
• Mol File: 1026701-89-2.mol
• Article Data: 3

Chemical Properties

• CAS DataBase Reference: C₂₂H₃₂N₂O₄S(CAS DataBase Reference)
• NIST Chemistry Reference: C₂₂H₃₂N₂O₄S(1026701-89-2)
• EPA Substance Registry System: C₂₂H₃₂N₂O₄S(1026701-89-2)

Safety Data

• Hazardous Substances Data: 1026701-89-2(Hazardous Substances Data)

Upstream product

• 98760-08-8 (1-oxiranyl-2-phenylethyl)carbamic acid tert-butyl ester 
• 34985-37-0 (S)-2-methylbutylamine 
• 1026701-65-4 N-[(1S,2R)-2-hydroxy-3-[((2S)-2-methylbutyl)amino]-1-(phenylmethyl)propyl]-carbamic acid 1,1-dimethylethyl ester 
• 1026701-52-9 N-[(1S,2R)-2-hydroxy-3-[[(4-methoxyphenyl)sulfonyl][(2S)-2-methylbutyl]amino]-1-(phenylmethyl)propyl]-carbamic acid 1,1-dimethylethyl ester 

Downstream Products

• 1066865-64-2 (R)-methyl 3-((((2S,3R)-3-hydroxy-4-(4-methoxy-N-((S)-2-methylbutyl)phenylsulfonamido)-1-phenylbutan-2-yl)carbamoyl)oxy)butanoate 
• 1066865-66-4 2-(2,2,2-trifluoroacetamido)ethyl ((2S,3R)-3-hydroxy-4-(4-methoxy-N-((S)-2-methylbutyl)phenylsulfonamido)-1-phenylbutan-2-yl)carbamate 
• 1066865-61-9 2-(2,2-dichloroacetamido)ethyl (2S,3R)-3-hydroxy-4-(4-methoxy-N-((S)-2-methylbutyl)phenylsulfonamido)-1-phenylbutan-2-ylcarbamate 
• 1066865-59-5 (R)-5-oxohexan-2-yl ((2S,3R)-3-hydroxy-4-(4-methoxy-N-((S)-2-methylbutyl)phenylsulfonamido)-1-phenylbutan-2-yl)carbamate 
• 1386394-57-5 2-((tert-butoxycarbonyl)amino)ethyl ((2S,3R)-3-hydroxy-4-(4-methoxy-N-((S)-2-methylbutyl)phenylsulfonamido)-1-phenylbutan-2-yl)carbamate 
• 1386394-58-6 (R)-methyl 3-((((2S,3R)-3-hydroxy-4-(4-methoxy-N-((S)-2-methylbutyl)phenylsulfonamido)-1-phenylbutan-2-yl)carbamoyl)oxy)-2-methylpropanoate 
• 1386394-59-7 2-(2-oxoimidazolidin-1-yl)ethyl ((2S,3R)-3-hydroxy-4-(4-methoxy-N-((S)-2-methylbutyl)phenylsulfonamido)-1-phenylbutan-2-yl)carbamate 
• 1386394-60-0 2-(2-oxooxazolidin-3-yl)ethyl ((2S,3R)-3-hydroxy-4-(4-methoxy-N-((S)-2-methylbutyl)phenylsulfonamido)-1-phenylbutan-2-yl)carbamate 
• 1066865-68-6 (R)-2-oxotetrahydrofuran-3-yl ((2S,3R)-3-hydroxy-4-(4-methoxy-N-((S)-2-methylbutyl)phenylsulfonamido)-1-phenylbutan-2-yl)carbamate 
• 1386394-61-1 ((S)-5-oxopyrrolidin-2-yl)methyl ((2S,3R)-3-hydroxy-4-(4-methoxy-N-((S)-2-methylbutyl)phenylsulfonamido)-1-phenylbutan-2-yl)carbamate 
• 1066865-56-2 3,4-dihydroxy-N-[(1S,2R)-2-hydroxy-3-[[(4-methoxyphenyl)sulfonyl][(2S)-2-methylbutyl]amino]-1-(phenylmethyl)propyl]benzamide 
• 1066869-48-4 (5S)-3-(3-acetylphenyl)-N-[(1S,2R)-2-hydroxy-3-[[(4-methoxyphenyl)sulfonyl][(2S)-2-methylbutyl]amino]-1-(phenylmethyl)propyl]-2-oxo-oxazolidine-5-carboxamide 

Relevant articles and documents

Substrate envelope-designed potent HIV-1 protease inhibitors to avoid drug resistance

Summary The rapid evolution of HIV under selective drug pressure has led to multidrug resistant (MDR) strains that evade standard therapies. We designed highly potent HIV-1 protease inhibitors (PIs) using the substrate envelope model, which confines inhib

HIV-1 protease inhibitors from inverse design in the substrate envelope exhibit subnanomolar binding to drug-resistant variants

The acquisition of drug-resistant mutations by infectious pathogens remains a pressing health concern, and the development of strategies to combat this threat is a priority. Here we have applied a general strategy, inverse design using the substrate envelope, to develop inhibitors of HIV-1 protease. Structure-based computation was used to design inhibitors predicted to stay within a consensus substrate volume in the binding site. Two rounds of design, synthesis, experimental testing, and structural analysis were carried out, resulting in a total of 51 compounds. Improvements in design methodology led to a roughly 1000-fold affinity enhancement to a wild-type protease for the best binders, from a Ki of 30-50 nM in round one to below 100 pM in round two. Crystal structures of a subset of complexes revealed a binding mode similar to each design that respected the substrate envelope in nearly all cases. All four best binders from round one exhibited broad specificity against a clinically relevant panel of drug-resistant HIV-1 protease variants, losing no more than 6-13-fold affinity relative to wild type. Testing a subset of second-round compounds against the panel of resistant variants revealed three classes of inhibitors: robust binders (maximum affinity loss of 14-16-fold), moderate binders (35-80-fold), and susceptible binders (greater than 100-fold). Although for especially high-affinity inhibitors additional factors may also be important, overall, these results suggest that designing inhibitors using the substrate envelope may be a useful strategy in the development of therapeutics with low susceptibility to resistance.