title: Targeting the dimerization interface for irreversible inhibition of HIV-1 protease.
abstract: A novel strategy was used to irreversibly inhibit HIV-1 protease. The inhibitor was designed to form a disulfide bond with Cys95, present at the dimerization interface of HIV-1 protease. The inhibitor was shown to be active against HIV-1 protease with K(inact) = 3.7 microM and V(inact) = 0.012 min(-1).
authors.affiliation: Department of Chemistry, Purdue University, West Lafayette, IN 47907, USA.
authors.forename: R
authors.initials: R
authors.lastname: Zutshi
authors.forename: J
authors.initials: J
authors.lastname: Chmielewski
mesh_terms: D019281:Dimerization; D016333:HIV Protease / Q000737:chemistry*; D017320:HIV Protease Inhibitors / Q000494:pharmacology*; D013329:Structure-Activity Relationship
chemical_list: D017320:HIV Protease Inhibitors; D016333:HIV Protease