DI-UMONS : Dépôt institutionnel de l’université de Mons

Recherche transversale
(titres de publication, de périodique et noms de colloque inclus)
2002-09-15 - Article/Dans un journal avec peer-review - Anglais - 6 page(s)

Gossuin Yves , Roch Alain , Muller Robert , Gillis Pierre , Lo Bue Francesco , "Anomalous Nuclear Magnetic Relaxation of Aqueous Solutions of Ferritin: An Unprecedented First-Order Mechanism" in Magnetic Resonance in Medicine : Official Journal of the Society of Magnetic Resonance in Medicine, 48, 959-964, DOI 10.1002/mrm.10316

  • Edition : Wiley Liss, Inc., New York (NY)
  • Codes CREF : Résonance magnétique nucléaire (biophysique) (DI131B), Biophysique (DI3113), Imagerie médicale, radiologie, tomographie (DI3243)
  • Unités de recherche UMONS : Physique expérimentale et biologique (M104), Chimie générale, organique et biomédicale (M108)
Texte intégral :

Abstract(s) :

(Anglais) Ferritin, the iron-storing protein, speeds up proton transverse magnetic relaxation in aqueous solutions. This T2 shortening is used in MRI to quantify iron in the brain and liver. Current theoretical models underestimate the relaxation enhancement by ferritin at imaging fields, and they do not predict the measured dependence of the rate enhancement on the magnetization of the particles. Here it is shown that a proton exchange dephasing model (PEDM) overcomes these limitations by allowing a first order relaxation mechanism. The PEDM considers proton exchange between bulk water and exchangeable protons located at the surface of the hydrated iron oxide nanometric core of the protein. Relaxation is shown to depend on the distribution of the frequency shifts of the adsorption sites; the observed properties agree with a Lorentzian distribution. Computer simulations utilizing recent Mössbauer spectroscopy data show that the distribution of these shifts is effectively Lorentzian.