Journal
BIOMATERIALS
Volume 33, Issue 21, Pages 5423-5430Publisher
ELSEVIER SCI LTD
DOI: 10.1016/j.biomaterials.2012.03.055
Keywords
Protein cages; Antibody-binding; Fc-binding peptide; Delivery platform; Molecular recognition
Funding
- Basic Science Research Program [2011-0004010]
- Advanced Research Center [20110000883]
- Biosignal Analysis Technology Innovation Program [2011-0027722]
- MEST through NRF of Korea [2011-0019464]
- National Research Foundation of Korea [2010-0009004, 2010-0019926] Funding Source: Korea Institute of Science & Technology Information (KISTI), National Science & Technology Information Service (NTIS)
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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. (C) 2012 Elsevier Ltd. All rights reserved.
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