Switching between allosteric and dimerization inhibition of HIV-1 protease

Michael J Bowman; Simon Byrne; Jean Chmielewski

doi:10.1016/j.chembiol.2005.02.004

Switching between allosteric and dimerization inhibition of HIV-1 protease

Chem Biol. 2005 Apr;12(4):439-44. doi: 10.1016/j.chembiol.2005.02.004.

Authors

Michael J Bowman¹, Simon Byrne, Jean Chmielewski

Affiliation

¹ Department of Chemistry, Purdue University, West Lafayett, Indiana 47907, USA.

PMID: 15850980
DOI: 10.1016/j.chembiol.2005.02.004

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.

Publication types

Research Support, U.S. Gov't, P.H.S.

MeSH terms

Amides / chemistry
Binding, Competitive / drug effects
HIV Protease / chemistry*
HIV Protease Inhibitors / chemistry*
HIV Protease Inhibitors / pharmacology*
Humans
Hydrogen Bonding
Kinetics
Models, Molecular
Phenethylamines / chemistry
Protein Binding
Spectrometry, Fluorescence
Stereoisomerism
Structure-Activity Relationship

Substances

Amides
HIV Protease Inhibitors
Phenethylamines
HIV Protease