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Studies on the interaction between docetaxel and human hemoglobin by spectroscopic analysis and molecular docking

Paper ID Volume ID Publish Year Pages File Format Full-Text
30914 44514 2011 7 PDF Available
Title
Studies on the interaction between docetaxel and human hemoglobin by spectroscopic analysis and molecular docking
Abstract

The binding reaction between docetaxel (DTX) and human hemoglobin (HHb) was investigated systematically with various spectroscopic methods including fluorescence quenching technique, ultraviolet (UV)–vis absorption, synchronous fluorescence, circular dichroism (CD) and Fourier transform infrared (FT-IR) spectroscopy. Analysis of fluorescence data showed that the quenching mechanism was the dynamic quenching and each protein had only one binding site for the drug. Two thermodynamic parameters, the enthalpy change and the entropy change were calculated to be 9.18 kJ mol−1 and 116 J mol−1 K−1, respectively, which suggested that hydrophobic interaction played a major role in the binding reaction. The results from different spectroscopic methods also showed that DTX could induce conformational changes of HHb. The molecular docking simulation demonstrated that DTX was located in the central cavity of HHb.

► We study the interaction between DTX and HHb by different spectroscopic techniques. ► The quenching mechanism was a dynamic quenching. ► There was only one binding site on HHb for DTX. ► Thermodynamic parameters suggested that hydrophobic interaction was a major force. ► The conformation of protein changed was induced by DTX.

Keywords
Docetaxel; Human hemoglobin; Interaction; Spectroscopy; Molecular docking
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Studies on the interaction between docetaxel and human hemoglobin by spectroscopic analysis and molecular docking
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Publisher
Database: Elsevier - ScienceDirect
Journal: Journal of Photochemistry and Photobiology B: Biology - Volume 105, Issue 2, 3 November 2011, Pages 126–132
Authors
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Subjects
Physical Sciences and Engineering Chemical Engineering Bioengineering
Get Full-Text Now
Don't Miss Today's Special Offer
Price was $35.95
You save - $31
Price after discount Only $4.95
100% Money Back Guarantee
Full-text PDF Download
Online Support
Any Questions? feel free to contact us