Recombinant fragment of an antibody tailored for direct radioiodination

Authors

  • Juraj Sedláček,

    1. Laboratory of Structural Biology, Institute of Molecular Genetics, Academy of Sciences of the Czech Republic, Praha 6 CZ, Czech Republic
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  • Milan Fábry,

    1. Laboratory of Structural Biology, Institute of Molecular Genetics, Academy of Sciences of the Czech Republic, Praha 6 CZ, Czech Republic
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  • Irena Sieglová,

    1. Laboratory of Structural Biology, Institute of Molecular Genetics, Academy of Sciences of the Czech Republic, Praha 6 CZ, Czech Republic
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  • Vlastimil Král,

    1. Laboratory of Structural Biology, Institute of Molecular Genetics, Academy of Sciences of the Czech Republic, Praha 6 CZ, Czech Republic
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  • Bronislava Uhnáková,

    1. Laboratory of Structural Biology, Institute of Molecular Genetics, Academy of Sciences of the Czech Republic, Praha 6 CZ, Czech Republic
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    • Present address: Department of Biogenesis and Biotechnology of Natural Compounds, Institute of Microbiology, Academy of Sciences of the Czech Republic, Praha 4, Czech Republic.
  • Marcela Múdra,

    1. Department of Biochemistry and Structural Biology, Institute of Molecular Biology, Slovak Academy of Sciences, Bratislava, Slovakia
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    • Present address: Faculty of Natural Sciences, Comenius University, Bratislava, Slovakia.
  • Leo Kronrád,

    1. Division of Radiopharmaceuticals, Nuclear Research Institute Řež plc., Řež near Prague, Czech Republic
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  • Agnieszka Sawicka,

    1. Polatom - Radioisotope Centre, Otwock, Poland
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  • Renata Mikolajczak,

    1. Polatom - Radioisotope Centre, Otwock, Poland
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  • Pavlína Řezáčová

    Corresponding author
    • Laboratory of Structural Biology, Institute of Molecular Genetics, Academy of Sciences of the Czech Republic, Praha 6 CZ, Czech Republic
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Pavlína Řezáčová, Laboratory of Structural Biology, Institute of Molecular Genetics, Academy of Sciences of the Czech Republic, Praha 4, Czech Republic.

E-mail: rezacova@img.cas.cz

Abstract

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This article presents the design and preparation of a single-chain variable fragment (scFv) of an antibody comprising an auxiliary polypeptide segment that is rich in tyrosine. This protein shows a higher capacity to bind iodine radionuclide, as compared with the parental scFv. The tyrosine-rich segment of the tailored protein is less hydrophobic (i.e. more solvent exposed) and can thus contribute to a redirection of the label from potentially sensitive scFv tyrosine residues.

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