Literature DB >> 16481905

Species dependence on plasma protein binding and relaxivity of the gadolinium-based MRI contrast agent MS-325.

Harriet B Eldredge1, Marga Spiller, Jaclyn M Chasse, Matthew T Greenwood, Peter Caravan.   

Abstract

RATIONALE AND
OBJECTIVES: We sought to determine whether there is a species dependence on plasma protein and serum album binding and/or relaxivity of the MR contrast agent MS-325.
METHODS: Equilibrium binding of MS-325 to plasma proteins or purified serum albumin was determined as a function of chelate concentration. T1 and T2 values were determined at 0.47 and 1.41 T, and NMRD profiles were measured to determine the changes in relaxivity over varying field strengths from 0.002 to 1.2 T.
RESULTS: The binding of MS-325 to either animal plasma or serum albumin plateaus at chelate concentrations less than 0.1 mM with human, pig, and rabbit plasmas showing maximum binding. Human and pig plasmas show the greatest observed relaxivity enhancement in the presence of MS-325.
CONCLUSIONS: MS-325 exhibits increased relaxivity in blood plasma as the result of plasma protein binding. Binding ranged from 64% to 91% and was species dependent: human > pig approximately rabbit > dog approximately rat approximately mouse.

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Year:  2006        PMID: 16481905     DOI: 10.1097/01.rli.0000199293.86956.48

Source DB:  PubMed          Journal:  Invest Radiol        ISSN: 0020-9996            Impact factor:   6.016


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