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Physicochemical Characterization of P760, a New Macromolecular Contrast Agent with High Relaxivity
Author(s) -
Vander Elst Luce,
Port Marc,
Raynal Isabelle,
Simonot Christian,
Muller Robert N.
Publication year - 2003
Publication title -
european journal of inorganic chemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.667
H-Index - 136
eISSN - 1099-0682
pISSN - 1434-1948
DOI - 10.1002/ejic.200300036
Subject(s) - chemistry , relaxometry , europium , gadolinium , rotational correlation time , aqueous solution , dota , proton , lanthanide , relaxation (psychology) , mri contrast agent , analytical chemistry (journal) , nuclear magnetic resonance , inorganic chemistry , molecule , spin echo , chromatography , ion , chelation , organic chemistry , medicine , social psychology , psychology , physics , quantum mechanics , magnetic resonance imaging , radiology
P760‐Gd, a hydrophilic derivative of DOTA‐Gd with a molecular mass of 5.6 kDa, has been characterized in various media: aqueous solution, protein‐containing solution, and Zn 2+ ‐containing solution. Several investigations have been carried out, including the determination of the number of inner‐sphere water molecules by laser‐induced luminescence of the europium complex, water 1 H nuclear magnetic relaxation rates as a function of field strength, and 17 O relaxometry of water of the gadolinium complex, pulsed magnetic field gradient spin echo of proton, and 2 H transverse relaxation rates of the labeled lanthanum analogue. The large proton relaxivity of P760‐Gd in water results from the long rotational correlation time of the hydrated complex (τ R ≈ 2 ns at 310 K). As with DOTA‐Gd, no significant Zn 2+ transmetallation process was observed by proton relaxometry. Finally, analysis of the non‐covalent binding of P760‐Gd to serum proteins by proton relaxometry showed that P760‐Gd does not interact with human serum albumin. (© Wiley‐VCH Verlag GmbH & Co. KGaA, 69451 Weinheim, Germany, 2003)