title: Heterocyclic HIV-1 protease inhibitors.
abstract: [formula: see text] A series of simple heterocyclic HIV-1 protease inhibitors were developed on the basis of size, shape, and electronic complementarity to the active site of the enzyme. The C2-symmetric heterocycles do not contain a transition-state isostere nor are they active site directed irreversible inhibitors; thus, they represent the success of a new design strategy. The first generation heterocycles inhibit the protease in the micromolar range, whereas control compounds show no bioactivity at the same concentrations.
authors.affiliation: Department of Chemistry, Kansas State University, Manhattan 66506, USA. baures@ksu.edu
authors.forename: P W
authors.initials: PW
authors.lastname: Baures
mesh_terms: D018360:Crystallography, X-Ray; D015195:Drug Design; D017320:HIV Protease Inhibitors / Q000138:chemical synthesis* / Q000737:chemistry; D006571:Heterocyclic Compounds / Q000138:chemical synthesis* / Q000737:chemistry; D008958:Models, Molecular; D009842:Oligopeptides / Q000737:chemistry
chemical_list: D017320:HIV Protease Inhibitors; D006571:Heterocyclic Compounds; D009842:Oligopeptides