Abstract
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.
Publication types
-
Research Support, U.S. Gov't, P.H.S.
MeSH terms
-
Combinatorial Chemistry Techniques
-
Cross-Linking Reagents / chemistry
-
Dimerization
-
HIV Protease / chemistry*
-
HIV Protease / genetics
-
HIV Protease Inhibitors / chemical synthesis*
-
HIV Protease Inhibitors / chemistry
-
Models, Molecular
-
Molecular Weight
-
Mutation
-
Oligopeptides / chemical synthesis*
-
Oligopeptides / chemistry
-
Structure-Activity Relationship
Substances
-
Cross-Linking Reagents
-
HIV Protease Inhibitors
-
Oligopeptides
-
HIV Protease