[Thermodynamic analysis of dimerization inhibitors binding to HIV protease monomers]

P V Ershov; O V Gnedenko; A A Mol'nar; A V Lisitsa; A S Ivanov; A I Archakov

doi:10.18097/pbmc20125801043

[Thermodynamic analysis of dimerization inhibitors binding to HIV protease monomers]

Biomed Khim. 2012 Jan-Feb;58(1):43-9. doi: 10.18097/pbmc20125801043.

[Article in Russian]

Authors

P V Ershov, O V Gnedenko, A A Mol'nar, A V Lisitsa, A S Ivanov, A I Archakov

PMID: 22642151
DOI: 10.18097/pbmc20125801043

Abstract

Here, we describe the analysis of kinetic and thermodynamic parameters for binding of peptide and nonpeptide dimerization inhibitors to immobilized HIV protease (HIVp) monomers by using surface plasmon resonance. Molecular interactions were investigated at different inhibitors concentrations (0-80 microM) and temperatures (15-35 degrees C). The kinetic, equilibrium and thermodynamic parameters have been determined. It was found that both inhibitors were characterized by similar interaction parameters. The complex formation is entropically driven process for both inhibitors. The entropic term(-TdeltaS) had the value about -20 kcal/mol while the enthalpic term (deltaH) had the positive value about 14 kcal/mol and counteracted the complex formation.

Publication types

English Abstract

MeSH terms

Dimerization
HIV Protease / chemistry*
HIV Protease Inhibitors / chemistry*
Humans
Kinetics
Protein Binding
Protein Multimerization / drug effects*
Surface Plasmon Resonance / methods*
Thermodynamics

Substances

HIV Protease Inhibitors
HIV Protease