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

Recherche transversale
(titres de publication, de périodique et noms de colloque inclus)
2010-01-01 - Article/Dans un journal avec peer-review - Anglais - 9 page(s)

Henoumont Céline , Vander Elst Luce , Laurent Sophie , Muller Robert , "Synthesis and physicochemical characterization of Gd-C4-thyroxin-DTPA, a potential MRI contrast agent. Evaluation of its affinity for human serum albumin by proton relaxometry, NMR diffusometry and electrospray mass spectrometry." in Journal of Physical Chemistry B, 114, 10, 3689-3697

  • Edition : American Chemical Society (DC)
  • Codes CREF : Résonance magnétique nucléaire (biophysique) (DI131B), Chimie organique (DI1313), Imagerie médicale, radiologie, tomographie (DI3243)
  • Unités de recherche UMONS : Chimie générale, organique et biomédicale (M108)
  • Instituts UMONS : Institut des Sciences et Technologies de la Santé (Santé), Institut des Biosciences (Biosciences)
Texte intégral :

Abstract(s) :

(Anglais) Gd-C4-thyroxin-DTPA, a potential MRI contrast agent, was synthesized from Gd-DTPA and thyroxine, which interacts strongly with human serum albumin (HSA). It was characterized in water by its relaxometric properties and its stability versus zinc transmetallation. The affinity of the complex for HSA was studied by three different methods: proton relaxometry, NMR diffusometry, and electrospray mass spectrometry. From the results it appears that Gd-C4-thyroxin-DTPA exhibits a relatively high relaxivity (r1 = 9.01 s-1 mM-1 at 1.5T and 310 K), a good stability versus zinc transmetallation, and a strong interaction with HSA (Ka ~ 10000 M-1 with 2 binding sites). The kinetics of the exchange between the bound and the free form of the complex was evaluated by the NMR diffusometry technique. Competition experiments have allowed the assignment of the chelate’s binding site on HSA.