Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
5402970 | Journal of Luminescence | 2009 | 8 Pages |
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 (ÎH0) and standard entropy (ÎS0) were calculated to be â41.07Â KJÂ molâ1 and â49.72Â JÂ molâ1Â Kâ1. 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
Related Topics
Physical Sciences and Engineering
Chemistry
Physical and Theoretical Chemistry
Authors
Hongxia Cheng, Hui Liu, Yuying Zhang, Guolin Zou,