This work is aimed at obtaining new insights into the design of novel Gd chelates that form high-affinity adducts with HSA. Two new Gd complexes that differ in the size of the hydrophobic moiety responsible for the interaction with the protein have been synthesised. It was shown that the two complexes protrude to a different extent from the surface of the protein (see picture), and this difference has an effect on the exchange of the coordinated water molecule.
New insights for pursuing high relaxivity MRI agents from modelling the binding interaction of Gd-III chelates to HSA
AIME, Silvio;GIANOLIO, Eliana;LONGO, DARIO LIVIO;
2005-01-01
Abstract
This work is aimed at obtaining new insights into the design of novel Gd chelates that form high-affinity adducts with HSA. Two new Gd complexes that differ in the size of the hydrophobic moiety responsible for the interaction with the protein have been synthesised. It was shown that the two complexes protrude to a different extent from the surface of the protein (see picture), and this difference has an effect on the exchange of the coordinated water molecule.
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