title: Switching between allosteric and dimerization inhibition of HIV-1 protease.
abstract: Refining the functional groups on a phenethylamine moiety within an inhibitor of HIV-1 protease led to a switch in the mechanism of inhibition from competitive and allosteric to dimerization inhibition. Phenylether extensions to the phenethylamine group led to agents that target the dimerization interface of HIV-1 protease with high potency.
authors.affiliation: Department of Chemistry, Purdue University, West Lafayett, Indiana 47907, USA.
authors.forename: Michael J
authors.initials: MJ
authors.lastname: Bowman
authors.forename: Simon
authors.initials: S
authors.lastname: Byrne
authors.forename: Jean
authors.initials: J
authors.lastname: Chmielewski
mesh_terms: D000577:Amides / Q000737:chemistry; D001667:Binding, Competitive / Q000187:drug effects; D016333:HIV Protease / Q000737:chemistry*; D017320:HIV Protease Inhibitors / Q000737:chemistry* / Q000494:pharmacology*; D006801:Humans; D006860:Hydrogen Bonding; D007700:Kinetics; D008958:Models, Molecular; D010627:Phenethylamines / Q000737:chemistry; D011485:Protein Binding; D013050:Spectrometry, Fluorescence; D013237:Stereoisomerism; D013329:Structure-Activity Relationship
chemical_list: D000577:Amides; D017320:HIV Protease Inhibitors; D010627:Phenethylamines; D016333:HIV Protease