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The number of primary binding sites, binding constant and physiological protein\u2010binding percentage were 1.9, 1.51\u00d710<jats:sup>3<\/jats:sup>\u2009M<jats:sup>\u22121<\/jats:sup> and 59.80%, respectively. In addition, the thermodynamic parameters including enthalpy change (\u0394<jats:italic>H<\/jats:italic>), entropy change (\u0394<jats:italic>S<\/jats:italic>) and free energy change (\u0394<jats:italic>G<\/jats:italic>) of the reaction were obtained in order to characterize the acting forces between doxycycline and HSA. Furthermore, to better understand the nature of doxycycline\u2013HSA binding and to get information about potential interaction with other drugs, displacement experiments were performed. The results showed that doxycycline binds at site II of HSA.<\/jats:p>","DOI":"10.1002\/elps.200800470","type":"journal-article","created":{"date-parts":[[2009,6,10]],"date-time":"2009-06-10T06:43:51Z","timestamp":1244616231000},"page":"1991-1997","source":"Crossref","is-referenced-by-count":25,"title":["Characterization of interaction between doxycycline and human serum albumin by capillary electrophoresis\u2010frontal 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