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Hong, Sung You
Synthetic Organic Chemistry Laboratory
Research Interests
  • Synthetic organic chemistry, transition metals, oxidation state

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Development of Protein-Cage-Based Delivery Nanoplatforms by Polyvalently Displaying beta-Cyclodextrins on the Surface of Ferritins Through Copper(I)-Catalyzed Azide/Alkyne Cycloaddition

Cited 8 times inthomson ciCited 3 times inthomson ci
Title
Development of Protein-Cage-Based Delivery Nanoplatforms by Polyvalently Displaying beta-Cyclodextrins on the Surface of Ferritins Through Copper(I)-Catalyzed Azide/Alkyne Cycloaddition
Author
Kwon, ChanhoKang, Young JiJeon, SangbinJung, SunhoHong, Sung YouKang, Sebyung
Keywords
β-cyclodextrins; Copper(I)-catalyzed azide/alkyne cycloaddition; Delivery nanoplatforms; Inclusion complexes; Protein cages
Issue Date
201211
Publisher
WILEY-V C H VERLAG GMBH
Citation
MACROMOLECULAR BIOSCIENCE, v.12, no.11, pp.1452 - 1458
Abstract
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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DOI
http://dx.doi.org/10.1002/mabi.201200178
ISSN
1616-5187
Appears in Collections:
SLS_Journal Papers
ECHE_Journal Papers
SBA_Journal Papers

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