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  • developing an antibody-binding protein cage as a molecular recognition drug modular nanoplatform

    جزئیات بیشتر مقاله
    • تاریخ ارائه: 1391/01/01
    • تاریخ انتشار در تی پی بین: 1391/01/01
    • تعداد بازدید: 572
    • تعداد پرسش و پاسخ ها: 0
    • شماره تماس دبیرخانه رویداد: -
     we genetically introduced the fc-binding peptide (fcbp) into the loop of a self-assembled protein cage, ferritin, constituting four-fold symmetry at the surface to use it as a modular delivery nanoplatform. fcbp-presenting ferritin (fcbp-ferritin) formed very stable non-covalent complexes with both human and rabbit iggs through the simple molecular recognition between the fc region of the antibodies and the fc-binding peptide clusters inserted onto the surface of fcbp-ferritin. this approach realized orientation-controlled display of antibodies on the surfaces of the protein cages simply by mixing without any complicated chemical conjugation. using trastuzumab, a human anti-her2 antibody used to treat patients with breast cancer, and a rabbit antibody to folate receptor, along with fluorescently labeled fcbp-ferritin, we demonstrated the specific binding of these complexes to breast cancer cells and folate receptor over-expressing cells, respectively, by fluorescent cell imaging. fcbp-ferritin may be potentially used as modular nanoplatforms for active targeted delivery vehicles or molecular imaging probes with a series of antibodies on demand.

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