Abstract
Affibody molecules represent a novel class of affinity proteins with a high potential as tracers for radionuclide molecular imaging. In this comparative structure–property study, a series of Affibody molecules with the 99mTc-chelators maGGG, maSSS, or maESE attached to the ε-amine of the internally positioned K49 was prepared by peptide synthesis, for comparison to molecules with similar chelators positioned at the N-terminus. The conjugates were labeled with 99mTc and evaluated in vitro and in vivo . It was found that both composition and position of the chelating moiety influence the label stability, biodistribution and targeting properties of HER2-binding Affibody molecules.
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