PMID- 22642151 OWN - NLM STAT- MEDLINE DCOM- 20120904 LR - 20191112 IS - 2310-6972 (Print) IS - 2310-6905 (Linking) VI - 58 IP - 1 DP - 2012 Jan-Feb TI - [Thermodynamic analysis of dimerization inhibitors binding to HIV protease monomers]. PG - 43-9 AB - 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. FAU - Ershov, P V AU - Ershov PV FAU - Gnedenko, O V AU - Gnedenko OV FAU - Mol'nar, A A AU - Mol'nar AA FAU - Lisitsa, A V AU - Lisitsa AV FAU - Ivanov, A S AU - Ivanov AS FAU - Archakov, A I AU - Archakov AI LA - rus PT - English Abstract PT - Journal Article PL - Russia (Federation) TA - Biomed Khim JT - Biomeditsinskaia khimiia JID - 101196966 RN - 0 (HIV Protease Inhibitors) RN - EC 3.4.23.- (HIV Protease) SB - IM MH - Dimerization MH - HIV Protease/*chemistry MH - HIV Protease Inhibitors/*chemistry MH - Humans MH - Kinetics MH - Protein Binding MH - Protein Multimerization/*drug effects MH - Surface Plasmon Resonance/*methods MH - Thermodynamics EDAT- 2012/05/31 06:00 MHDA- 2012/09/05 06:00 CRDT- 2012/05/31 06:00 PHST- 2012/05/31 06:00 [entrez] PHST- 2012/05/31 06:00 [pubmed] PHST- 2012/09/05 06:00 [medline] AID - 10.18097/pbmc20125801043 [doi] PST - ppublish SO - Biomed Khim. 2012 Jan-Feb;58(1):43-9. doi: 10.18097/pbmc20125801043.