Reference : Investigation of non-covalent interactions between paramagnetic complexes and human s...
Scientific journals : Article
Physical, chemical, mathematical & earth Sciences : Chemistry
http://hdl.handle.net/2268/347
Investigation of non-covalent interactions between paramagnetic complexes and human serum albumin by electrospray mass spectrometry
English
Henrotte, Virginie [Université de Mons-Hainaut > Département de Chimie Organique > Laboratoire de RMN > >]
Laurent, Sophie [Université de Mons-Hainaut > Département de Chimie Organique > Laboratoire de RMN >]
Gabelica, Valérie mailto [Université de Liège - ULg > Département de Chimie (Sciences) > Chimie physique, spectrométrie de masse >]
Vander Elst, Luce [Université de Mons-Hainaut > Département de Chimie Organique > Laboratoire de RMN > >]
De Pauw, Edwin mailto [Université de Liège - ULg > Département de Chimie (Sciences) > Chimie physique, spectrométrie de masse >]
Muller, Robert N [Université de Mons-Hainaut > Département de Chimie Organique > Laboratoire de RMN > >]
2004
Rapid Communications in Mass Spectrometry : RCM
John Wiley & Sons, Inc
18
17
1919-1924
Yes (verified by ORBi)
International
0951-4198
Chichester
United Kingdom
[en] mass spectrometry ; electrospray ; noncovalent interactions ; human serum albumin ; contrast agents ; MRI
[en] Stable gadolinium(III) chelates are nowadays routinely used as contrast agents for magnetic resonance imaging (MRI). Their non-covalent binding to human serum albumin (HSA) has shown to improve their efficacy. Non-covalent interactions lead to complex formation that can be quantified by several techniques that are mostly tedious and time-consuming. In this study, electrospray ionization mass spectrometry (ESI-MS) was used to investigate the interaction between HSA and several gadolinium(III) complexes. The results were compared with those obtained in the liquid phase. Four gadolinium complexes were investigated: Gd-DTPA 1, Gd-C4Me-DTPA 2, Gd-EOB-DTPA 3, and MP-2269 4. Relaxometry studies show that complexes 1 and 2 have no significant affinity for HSA, while complexes 3 and 4 have increasing affinities for the protein. 1:1 and 1:2 complexes between HSA and MP-2269 were detected by ESI-MS for a twofold excess of the contrast agent, whereas a ligand/protein molar ratio of 4:1 was necessary to observe a 1:1 stoichiometry for Gd-EOB-DTPA, an observation that is in good agreement with the known weaker affinity of the contrast agent for the protein. At a fourfold molar excess, no supramolecular complex was observed for Gd-DTPA I and Gd-C4Me-DTPA 2; a tenfold molar excess was necessary to detect a 1:1 complex, confirming the very weak affinity of these contrast agents for HSA.
Centre Interfacultaire d'Analyse des Résidus en Traces - CART
Fonds de la Recherche Scientifique (Communauté française de Belgique) - F.R.S.-FNRS
Researchers
http://hdl.handle.net/2268/347
10.1002/rcm.1571
http://www.interscience.wiley.com/
This is a preprint of an article published in Rapid Commun. Mass Spectrom. (2004), 18, 1919-1924.
© 2004 John Wiley & Sons Ltd.

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