Interaction between deferiprone and human serum albumin: Multi-spectroscopic, electrochemical and molecular docking methods

[Display omitted] The interactions between deferiprone (DEP) and human serum albumin (HSA) have been investigated systematically by fluorescence, Circular dichroism (CD) spectroscopy, UV–Vis absorption spectroscopy, electrochemistry and molecular modeling methods. The fluorescence quenching observed...

Full description

Saved in:
Bibliographic Details
Published in:European journal of pharmaceutical sciences 2014-11, Vol.64, p.9-17
Main Authors: Seyed Dorraji, M.S., Panahi Azar, V., Rasoulifard, M.H.
Format: Article
Language:English
Subjects:
Binding pattern
Circular Dichroism
Electrochemical Techniques
Fluorescence Resonance Energy Transfer
Human serum albumin
Humans
Interaction
Molecular docking
Molecular Docking Simulation
Pyridones - chemistry
Serum Albumin - chemistry
Spectrophotometry, Ultraviolet
Thermodynamics
Citations: Items that this one cites
Items that cite this one
Online Access:Get full text
Tags: Add Tag
No Tags, Be the first to tag this record!
Description
Summary:[Display omitted] The interactions between deferiprone (DEP) and human serum albumin (HSA) have been investigated systematically by fluorescence, Circular dichroism (CD) spectroscopy, UV–Vis absorption spectroscopy, electrochemistry and molecular modeling methods. The fluorescence quenching observed is attributed to the formation of a complex between HSA and DEP, and the reverse temperature effect of the fluorescence quenching has been found and discussed. The thermodynamic parameters, enthalpy changes (ΔH) and entropy change (ΔS) were calculated, according to the Van’t Hoff equation. These data suggested that hydrophobic interaction was the predominant intermolecular forces stabilizing the complex, which was in good agreement with the results of molecular modeling study. The primary binding pattern is determined by hydrophobic interaction occurring in Sudlow’s site I of HSA. DEP could slightly change the secondary structure and induce unfolding of the polypeptides of protein. An average binding distance of ∼2.88nm has been determined on the basis of the Förster’s resonance energy theory (FRET).
ISSN:0928-0987
1879-0720
DOI:10.1016/j.ejps.2014.08.001