Heterocyclic HIV-1 protease inhibitors.
[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.
Baures
P W
PW
Department of Chemistry, Kansas State University, Manhattan 66506, USA. baures@ksu.edu
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
D017320:HIV Protease Inhibitors; D006571:Heterocyclic Compounds; D009842:Oligopeptides