TAILIEUCHUNG - Báo cáo khoa học: Ibuprofen binding to secondary sites allosterically modulates the spectroscopic and catalytic properties of human serum heme–albumin

The ibuprofen primary binding site FA3–FA4 is located in domain III of human serum albumin (HSA), the secondary clefts FA2 and FA6 being sited in domains I and II. Here, the thermodynamics of ibuprofen binding to recombinant Asp1–Glu382 truncated HSA (tHSA)–heme-Fe(III) and nitrosylated tHSA–heme-Fe(II), encompassing domains I and II only, is reported. | IFEBS Journal Ibuprofen binding to secondary sites allosterically modulates the spectroscopic and catalytic properties of human serum heme-albumin Alessandra di Masi1 Francesca Gullotta2 3 Alessandro Bolli1 Gabriella Fanali4 Mauro Fasano4 and Paolo Ascenzi1 1 Department of Biology and InterdepartmentalLaboratory of Electron Microscopy University Roma Tre Italy 2 Department of ExperimentalMedicine and BiochemicalSciences University of Rome Tor Vergata Italy 3 Interuniversity Consortium for the Research on the Chemistry of Metals in BiologicalSystems Bari Italy 4 Department of Structuraland FunctionalBiology and Center of Neuroscience University of Insubria Busto Arsizio VA Italy Keywords allostery human serum heme-albumin ibuprofen binding modulation of reactivity and spectroscopic properties recombinant truncated human serum heme-albumin Asp1-Glu382 Correspondence P. Ascenzi Department of Biology and Interdepartmental Laboratory of Electron Microscopy University Roma Tre Viale Guglielmo Marconi 446 I-00146 Rome Italy Fax 39 06 5733 6321 Tel 39 06 5733 3200 2 E-mail ascenzi@ Received 14 July 2010 revised 24 November 2010 accepted 6 December 2010 The ibuprofen primary binding site FA3-FA4 is located in domain III of human serum albumin HSA the secondary clefts FA2 and FA6 being sited in domains I and II. Here the thermodynamics of ibuprofen binding to recombinant Asp1-Glu382 truncated HSA tHSA -heme-Fe III and nitrosylated tHSA-heme-Fe II encompassing domains I and II only is reported. Moreover the allosteric effect of ibuprofen on the kinetics of tHSA-heme-Fe III -mediated peroxynitrite isomerization and nitrosylated tHSA-heme-Fe II denitrosylation has been investigated. The present data indicate for the first time that the allosteric modulation of tHSA-heme and HSA-heme reactivity by ibuprofen depends mainly on drug binding to the FA2 and FA6 secondary sites rather than drug association with the FA3-FA4 primary cleft. Thus tHSA is a valuable model with .

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