期刊
JOURNAL OF LUMINESCENCE
卷 129, 期 10, 页码 1196-1203出版社
ELSEVIER SCIENCE BV
DOI: 10.1016/j.jlumin.2009.05.023
关键词
Docetaxel; Human serum albumin; Fluorescence quenching; Circular dichroism; FT-IR; Binding thermodynamics
类别
资金
- National Fund of Nature Science of China [20873092, 30800190, 30670464]
- Specialized Research Fund for the Doctoral Program of Higher Education (RFDP)
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 (Delta H-0) and standard entropy (Delta S-0) 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. (C) 2009 Elsevier B.V. All rights reserved.
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