Comparing the Interaction of Cyclophosphamide Monohydrate to Human Serum Albumin as Opposed to Holo-Transferrin by Spectroscopic and Molecular Modeling Methods: Evidence for Allocating the Binding Site

2010 ◽  
Vol 17 (12) ◽  
pp. 1524-1535 ◽  
Author(s):  
Shirin Hamed-Akbari Tousi ◽  
Mohammad Reza Saberi ◽  
Jamshidkhan Chamani
Keyword(s):  
Molecular Modeling ◽  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Binding Site ◽  
Modeling Methods

scholarly journals Investigation of the mechanism of binding of thiacloprid to human serum albumin using spectroscopic techniques and molecular modeling methods

2011 ◽  
Vol 25 (2) ◽  
pp. 113-122 ◽  
Author(s):  
Chuanxian Wang ◽  
Qinghua Chu ◽  
Changyun Chen ◽  
Zhao Bo
Keyword(s):  
Molecular Modeling ◽  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Electrostatic Interactions ◽  
Entropy Change ◽  
Binding Pocket ◽  
Cd Spectroscopy ◽  
Spectroscopic Techniques ◽  
Modeling Methods

Fluorescence spectroscopy, UV absorption, circular dichroism (CD) spectroscopy and molecular modeling methods were used to characterize the binding properties of thiacloprid (TL) with human serum albumin (HSA) at molecular level under physiological conditions. The fluorescence intensity of HSA decreased regularly with the gradually increasing concentration of thiacloprid. The binding constant K at three different temperatures (290, 300 and 310 K) were 3.07, 2.74 and 1.35 × 104M−1, respectively, for TL–HSA interaction have been calculated from the relevant fluorescence data. CD spectroscopic measurements have shown that the secondary structures of the protein have been changed by the interaction of thiacloprid with HSA. Furthermore, the study of molecular modeling indicated that thiacloprid could be located on the surface of the binding pocket of subdomains IIA in HSA. The hydrophobic interaction was the major acting force and there are H-bonds and electrostatic interactions between TL and HSA, which is in good agreement with the results from the experimental thermodynamic parameters (the enthalpy change ΔH0and the entropy change ΔS0were calculated to be -20.378 kJ/mol and 16.328 J/mol K according to the Van9t Hoff equation).

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