Title of article :
Interaction of the docetaxel with human serum albumin using optical spectroscopy methods
Author/Authors :
Hongxia Cheng، نويسنده , , Hui Liu، نويسنده , , Yuying Zhang، نويسنده , , Guolin Zou، نويسنده ,
Issue Information :
روزنامه با شماره پیاپی سال 2009
Pages :
8
From page :
1196
To page :
1203
Abstract :
Docetaxel is a semi-synthetic product derived from the needles of the European yew. It is an antineoplastic agent belonging to the taxoid family. The interaction between docetaxel and human serum albumin (HSA) has been investigated systematically by the fluorescence quenching technique, synchronous fluorescence spectroscopy, ultraviolet (UV)–vis absorption spectroscopy, circular dichroism (CD) spectroscopy and Fourier transform infrared (FT-IR) under physiological conditions. Our fluorescence data showed that HSA had only one docetaxel binding site and the binding process was a static quenching procedure. According to the Van’t Hoff equation, the thermodynamic parameters standard enthalpy (ΔH0) and standard entropy (ΔS0) were calculated to be −41.07 KJ mol−1 and −49.72 J mol−1 K−1. These results suggested that hydrogen bond was the predominant intermolecular force stabling the docetaxel–HSA complex. The data from the CD, FT-IR and UV–vis spectroscopy supported the change in the secondary structure of protein caused by the interaction of docetaxel with HSA.
Keywords :
Fluorescence quenching , circular dichroism , binding thermodynamics , FT-IR , docetaxel , human serum albumin
Journal title :
Journal of Luminescence
Serial Year :
2009
Journal title :
Journal of Luminescence
Record number :
1259650
Link To Document :
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