Multilocus Binding Increases the Relaxivity of Protein??Bound MRI Contrast Agents

…, TJ McMurry, RB Lauffer, P Caravan

Index: Zhang, Zhaoda; Greenfield, Matthew T.; Spiller, Marga; McMurry, Thomas J.; Lauffer, Randall B.; Caravan, Peter Angewandte Chemie - International Edition, 2005 , vol. 44, # 41 p. 6766 - 6769

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Citation Number: 114

Abstract

two protein-binding moieties. The DTPA moiety [13] shown in Figure 2 was used instead of the monoamide, because the GdDTPA complex has a more favorable water-exchange rate and the thermodynamically stable GdDTPA core is already present in several clinically approved contrast agents.[14] Human serum albumin (HSA) was chosen as the protein target for proof of principle and MS-325 (Figure 2) was used as a benchmark compound. ...