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

П. В. Ершов | Zendy; O.V. Gnedenko | Zendy; A. A. Molnar | Zendy; Andrey Lisitsa | Zendy; Ivanov As | Zendy; Alexander I. Archakov | Zendy

Open Access

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

Author(s) -

П. В. Ершов,

O.V. Gnedenko,

A. A. Molnar,

Andrey Lisitsa,

Ivanov As,

Alexander I. Archakov

Publication year - 2012

Publication title -

biomeditsinskaya khimiya

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 0.192

H-Index - 15

eISSN - 2310-6972

pISSN - 2310-6905

DOI - 10.18097/pbmc20125801043

Subject(s) - surface plasmon resonance , chemistry , hiv 1 protease , monomer , protease , kinetic energy , kinetics , resonance (particle physics) , peptide , hydrophobic effect , computational chemistry , enzyme , stereochemistry , organic chemistry , biochemistry , nanoparticle , nanotechnology , polymer , materials science , physics , particle physics , quantum mechanics

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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