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

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

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

Biomed Khim ; 58(1): 43-9, 2012.

Article en Ru | MEDLINE | ID: mdl-22642151

RESUMEN

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.

Asunto(s)

Inhibidores de la Proteasa del VIH/química; Proteasa del VIH/química; Multimerización de Proteína/efectos de los fármacos; Resonancia por Plasmón de Superficie/métodos; Dimerización; Humanos; Cinética; Unión Proteica; Termodinámica

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Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Proteasa del VIH / Inhibidores de la Proteasa del VIH / Resonancia por Plasmón de Superficie / Multimerización de Proteína Límite: Humans Idioma: Ru Revista: Biomed Khim Año: 2012 Tipo del documento: Article Pais de publicación: Rusia

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