Developing an antibody-binding protein cage as a molecular recognition drug modular nanoplatform
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- Developing an antibody-binding protein cage as a molecular recognition drug modular nanoplatform
- Kang, Hyo Jin; Kang, Young Ji; Lee, Young-Mi; Shin, Hyun-Hee; Chung, Sang J.; Kang, Sebyung
- Issue Date
- ELSEVIER SCI LTD
- BIOMATERIALS, v.33, no.21, pp.5423 - 5430
- 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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