Kinetic and Thermodynamic Analysis of Dimerization Inhibitors Binding to HIV Protease Monomers by Surface Plasmon Resonance

   
Ershov P.V.1 , Gnedenko O.V.1, Molnar A.A.1, Lisitsa A.V.1, Ivanov A.S.1, Archakov A.I.1

1. Institute of Biomedical Chemistry RAMS
Section: Experimental/Clinical Study
DOI: 10.18097/pbmc20125801043      UDK: 577.152.3.      PubMed Id: 22642151
Year: 2012  Volume: 58  Issue: 1  Pages: 43-49
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 μM) and temperatures (15-35°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(-ТΔS) had the value about -20 kcal/mol while the enthalpic term (ΔH) had the positive value about 14 kcal/mol and counteracted the complex formation.
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Ershov P.V., Gnedenko O.V., Molnar A.A., Lisitsa A.V., Ivanov A.S., Archakov A.I. (2012) Biomeditsinskaya khimiya, 58(1), 43-49.
This paper is also available as the English translation:10.1134/S1990750812010039
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