Contrast agents for magnetic resonance angiographic applications: 1H and 17O NMR relaxometric investigations on two gadolinium(III) DTPA-like chelates endowed with high binding affinity to human serum albumin |
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Authors: | S Aime Monica Chiaussa Giuseppe Digilio Eliana Gianolio Enzo Terreno |
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Institution: | (1) Dipartimento di Chimica Inorganica, Chimica Fisica e Chimica dei Materiali, Università di Torino via Pietro Giuria 7, I-10125 Turin, Italy e-mail: aime@silver.ch.unito.it >Tel.: +39-011-6707520, Fax: +39-011-6707524, IT |
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Abstract: | N,N′,N″,N‴ -pentaacetic acid) bearing different substituents for binding to human serum albumin (HSA) are compared. In spite of the structural
differences of the recognition synthon and of the residual electric charge, the two chelates display an analogous binding
affinity for the serum protein. Upon formation of the adducts with HSA, the exchange rates of the coordinated water appear
slowed down by an amount corresponding to ca. 50% of the rates found for the free complexes. The relaxivity of Gd(BOM)3DTPA (H2O)]2 − is significantly higher than that of MS-325 either in the free complex or in the macromolecular adduct. Finally, the effect
of pH on the stability of the HSA adducts and on the values of their relaxivities has been investigated.
Received: 11 June 1999 / Accepted: 15 September 1999 |
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Keywords: | Gadolinium(III) complexes Contrast agents Magnetic resonance imaging Human serum albumin Proton relaxation enhancement |
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