Development of low molecular weight HIV-1 protease dimerization inhibitors.
The role of HIV protease in viral replication has made it a significant target for inhibition. The focus of our studies is to target the dimerization interface of HIV-1 protease because disruption of the dimer will inhibit enzymatic activity. The initial strategy began with cross-linked peptides derived from the interface of HIV protease. Herein we describe the design of a focused library of agents based on a minimal pharmacophore for HIV-1 protease dimerization inhibition.
Hwang
You Seok
YS
Department of Chemistry, Purdue University, 560 Oval Drive, West Lafayette, Indiana 47907, USA.
Chmielewski
Jean
J
D020650:Combinatorial Chemistry Techniques; D003432:Cross-Linking Reagents / Q000737:chemistry; D019281:Dimerization; D016333:HIV Protease / Q000737:chemistry* / Q000235:genetics; D017320:HIV Protease Inhibitors / Q000138:chemical synthesis* / Q000737:chemistry; D008958:Models, Molecular; D008970:Molecular Weight; D009154:Mutation; D009842:Oligopeptides / Q000138:chemical synthesis* / Q000737:chemistry; D013329:Structure-Activity Relationship
D003432:Cross-Linking Reagents; D017320:HIV Protease Inhibitors; D009842:Oligopeptides; D016333:HIV Protease