679402-80-3

Upstream product

• 121-60-8 p-acetylaminobenzenesulfonyl chloride 
• 301210-56-0 (10S,13S,1'R)-13-[1'-hydroxy-2'-(1''-amino-3''-methylbutyl)ethyl]-8,11-dioxo-10-isopropyl-2-oxa-9,12-diazabicyclo[13.2.2]nonadeca-15,17,18-triene 
• 180078-30-2 (10S,13S,1'S)-13-(1'-hydroxy-2'-bromoethyl)-8,11-dioxo-10-isopropyl-2-oxa-9,12-diazabicyclo[13.2.2]nonadeca-15,17,18-triene 
• 180078-28-8 (10S,13S)-13-(1'-oxo-2'-bromoethyl)-8,11-dioxo-10-isopropyl-2-oxa-9,12-diazabicyclo[13.2.2]nonadeca-15,17,18-triene 
• 180078-26-6 (10S,13S)-13-(1'-oxo-2'-diazoethyl)-8,11-dioxo-10-isopropyl-2-oxa-9,12-diazabicyclo[13.2.2]nonadeca-15,17,18-triene 
• 180078-32-4 (10S,13S,1'S)-13-(1',2'-epoxyethyl)-8,11-dioxo-10-isopropyl-2-oxa-9,12-diazabicyclo[13.2.2]nonadeca-15,17,18-triene 
• 180078-24-4 10S-isopropyl-8,11-dioxo-2-oxa-9,12-diaza-bicyclo[13.2.2]nonadeca-1⁽¹⁸⁾,15⁽¹⁹⁾,16-triene-13S-carboxylic acid 
• 107-85-7 1-amino-3-methylbutane 

Relevant academic research and scientific papers

Countering Cooperative Effects in Protease Inhibitors Using Constrained β-Strand-Mimicking Templates in Focused Combinatorial Libraries

A major problem in de novo design of enzyme inhibitors is the unpredictability of the induced fit, with the shape of both ligand and enzyme changing cooperatively and unpredictably in response to subtle structural changes within a ligand. We have investig

Synthesis, stability, antiviral activity, and protease-bound structures of substrate-mimicking constrained macrocyclic inhibitors of HIV-1 protease

Three new peptidomimetics (1-3) have been developed with highly stable and conformationally constrained macrocyclic components that replace tripeptide segments of protease substrates. Each compound inhibits both HIV-1 protease and viral replication (HIV-1