Journal
MACROMOLECULAR BIOSCIENCE
Volume 12, Issue 11, Pages 1452-1458Publisher
WILEY-V C H VERLAG GMBH
DOI: 10.1002/mabi.201200178
Keywords
copper(I)-catalyzed azide/alkyne cycloaddition; beta-cyclodextrins; delivery nanoplatforms; inclusion complexes; protein cages
Funding
- MEST through NRF of Korea [2011-0004010, 2011-0014664]
- Korea Research Council of Fundamental Science and Technology (KRCF) [Seed-11-6]
- UNIST (Ulsan National Institute of Science and Technology)
- National Research Council of Science & Technology (NST), Republic of Korea [Seed-11-6] Funding Source: Korea Institute of Science & Technology Information (KISTI), National Science & Technology Information Service (NTIS)
- National Research Foundation of Korea [2011-0014664] Funding Source: Korea Institute of Science & Technology Information (KISTI), National Science & Technology Information Service (NTIS)
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Protein cages are spherical hollow macromolecules that are attractive platforms for the construction of nanoscale cargo delivery vehicles. Human heavy-chain ferritin (HHFn) is modified genetically to control the number and position of functional groups per cage. 24 beta-CDs are conjugated precisely to the modified HHFn in specific locations through thiol-maleimide Michael-type addition followed by copper(I)-catalyzed azide/alkyne cycloaddition (CuAAC). The resulting human ferritins displaying beta-CDs (beta-CD-C90 HHFn) can form inclusion complexes with FITC-AD, which can slowly release the guest molecule reversibly in a buffer solution via non-covalent beta-CD/AD interactions. beta-CD-C90 HHFn can potentially be used as delivery vehicles for insoluble drugs.
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