Acta Phys. -Chim. Sin. ›› 2009, Vol. 25 ›› Issue (10): 2147-2154.doi: 10.3866/PKU.WHXB20091112

• ARTICLE • Previous Articles     Next Articles

Characterization of the Interactions between Itraconazole and Human and Bovine Serum Albumins by a Spectroscopic Method

GUO Qing-Lian, LI Ran, JIANG Feng-Lei, TU Jian-Cheng, LI Lin-Wei, LIU Yi   

  1. Zhongnan Hospital, Wuhan University, Wuhan 430071, P. R. China|State Key Laboratory of Virology &|Key Laboratory of Analytic Chemistry for Biology and Medicine of Ministry of Education, College of Chemistry and Molecular Sciences, Wuhan University, Wuhan 430072, P. R. China|College of Chemistry and Chemical Engineering, Liaocheng University, Liaocheng 252059, Shandong Province, P. R. China
  • Received:2009-07-20 Revised:2009-08-28 Published:2009-09-29
  • Contact: TU Jian-Cheng E-mail:Jian_1999@yahoo.com

Abstract:

The binding of itraconazole (ITZ), a potential antifungal, to human serumalbumin (HSA) and bovine serum albumin (BSA) were studied at the physiological acidity (pH=7.4±0.1) by fluorescence and UV-Vis spectroscopies. A decrease in the quenching constant was observed with an increase in temperature. From the fluorescence spectrum and the fluorescence intensity, we observed that ITZ strongly quenches the intrinsic fluorescence of both BSA and HSA by static quenching. Thermodynamic parameters, such as △G, △H and △S, were calculated at different temperatures, showing that electrostatic and hydrophobic interactions were mostly responsible for the binding of ITZ to serum albumin. The distance d between the donor (HAS or BSA ) and acceptor (ITZ) was obtained according to fluorescence resonance energy transfer theory (FRET). Synchronous fluorescence and UV-Vis spectroscopy clearly revealed that the microenvironment and the conformation of serumalbumins changed during the binding reaction.

Key words: Thermodynamic parameter, Itraconazole, Bovine serumalbumin, Human serumalbumin, Fluorescence quenching, UV-Vis spectroscopy

MSC2000: 

  • O644