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Evaluation of Maleimide Derivative of DOTA for Site-Specific Labeling of Recombinant Affibody Molecules

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Division of Nuclear Medicine, Department of Medical Sciences, Uppsala University, Uppsala, Sweden, Affibody AB, Bromma, Sweden, Division of Biomedical Radiation Sciences, Rudbeck Laboratory, Uppsala University, Uppsala, Sweden, Hospital Physics, Department of Oncology, Uppsala University Hospital, Uppsala, Sweden
* Communicating author. Vladimir Tolmachev, Biomedical Radiation Sciences, Rudbeck Laboratory, Uppsala University, S-751 81 Uppsala, Sweden. Phone: +46 18 471 3414 , Fax: + 46 18 471 3432, [email protected].
†Department of Medical Sciences, Uppsala University.
‡Affibody AB.
§Rudbeck Laboratory, Uppsala University.
∥Department of Oncology, Uppsala University Hospital.
Cite this: Bioconjugate Chem. 2008, 19, 1, 235–243
Publication Date (Web):December 29, 2007
https://doi.org/10.1021/bc700307y
Copyright © 2008 American Chemical Society
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    Abstract

    Affibody molecules are a new class of small (7 kDa) scaffold affinity proteins, which demonstrate promising properties as agents for in vivo radionuclide targeting. The Affibody scaffold is cysteine-free and therefore independent of disulfide bonds. Thus, a single thiol group can be engineered into the protein by introduction of one cysteine. Coupling of thiol-reactive bifunctional chelators can enable site-specific labeling of recombinantly produced Affibody molecules. In this study, the use of 1,4,7,10-tetraazacyclododecane-1,4,7-tris-acetic acid-10-maleimidoethylacetamide (MMA-DOTA) for 111In-labeling of anti-HER2 Affibody molecules His6-ZHER2:342-Cys and ZHER2:2395-Cys has been evaluated. The introduction of a cysteine residue did not affect the affinity of the proteins, which was 29 pM for His6-ZHER2:342-Cys and 27 pM for ZHER2:2395-Cys, comparable with 22 pM for the parental ZHER2:342. MMA-DOTA was conjugated to DTT-reduced Affibody molecules with a coupling efficiency of 93% using a 1:1 molar ratio of chelator to protein. The conjugates were labeled with 111In to a specific radioactivity of up to 7 GBq/mmol, with preserved binding for the target HER2. In vivo, the non-His-tagged variant 111In-[MMA-DOTA-Cys61]-ZHER2:2395-Cys demonstrated appreciably lower liver uptake than its His-tag-containing counterpart. In mice bearing HER2-expressing LS174T xenografts, 111In-[MMA-DOTA-Cys61]-ZHER2:2395-Cys showed specific and rapid tumor localization, and rapid clearance from blood and nonspecific compartments, leading to a tumor-to-blood-ratio of 18 ± 8 already 1 h p.i. Four hours p.i., the tumor-to-blood ratio was 138 ± 8. Xenografts were clearly visualized already 1 h p.i.

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