Osteopontin: A Uranium Phosphorylated Binding-Site Characterization - IN2P3 - Institut national de physique nucléaire et de physique des particules Access content directly
Journal Articles Chemistry - A European Journal Year : 2013

Osteopontin: A Uranium Phosphorylated Binding-Site Characterization

S. Safi
  • Function : Author
G. Creff
C. Basset
  • Function : Author
P. Lorenzo Solari
  • Function : Author
C. Vidaud
  • Function : Author


Herein, we describe the structural investigation of one possible uranyl binding site inside a nonstructured protein. This approach couples spectroscopy, thermodynamics, and theoretical calculations (DFT) and studies the interaction of uranyl ions with a phosphopeptide, thus mimicking a possible osteopontin (OPN) hydroxyapatite growth-inhibition site. Although thermodynamical aspects were investigated by using time-resolved laser fluorescence spectroscopy (TRLFS) and isothermal titration calorimetry (ITC), structural characterization was performed by extended X-ray absorption fine structure (EXAFS) at the U LIII-edge combined with attenuated total reflection Fourier transform infrared (ATR-FTIR) spectroscopy. From the vibrational and fluorescence spectra, several structural models of a UO22+/peptide complex were developed and subsequently refined by using theoretical calculations to fit the experimental EXAFS obtained. The structural effect of the pH value was also considered under acidic to moderately acidic conditions (pH 1.5-5.5). Most importantly, the uranyl/peptide coordination environment was similar to that of the native protein.

Dates and versions

in2p3-00909073 , version 1 (25-11-2013)



S. Safi, G. Creff, A. Jeanson, C. Basset, J. Roques, et al.. Osteopontin: A Uranium Phosphorylated Binding-Site Characterization. Chemistry - A European Journal, 2013, 19, pp.11261-11269. ⟨10.1002/chem.201300989⟩. ⟨in2p3-00909073⟩
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