Journal
JOURNAL OF THE AMERICAN CHEMICAL SOCIETY
Volume 137, Issue 47, Pages 14838-14841Publisher
AMER CHEMICAL SOC
DOI: 10.1021/jacs.5b09711
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Funding
- Department of Defense National Security Science and Engineering Faculty Fellowship [N00014-15-1-0043]
- Center for Cancer Nanotechnology Excellence initiative of the National Institutes of Health [U54 CATS 1880]
- NTU-NU Institute for NanoMedicine located at the Intl. Inst. for Nanotechnology, Northwestern University, U.S.A.
- Nanyang Technological University, Singapore
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We report a strategy for creating a new class of protein transfection materials composed of a functional protein core chemically modified with a dense shell of oligonucleotides. These materials retain the native structure and catalytic ability of the hydrolytic enzyme beta-galactosidase, which serves as the protein core, despite the functionalization of its surface with 15 DNA strands. The covalent attachment of a shell of oligonudeotides to the surface of beta-galactosidase enhances its cellular uptake of by up to similar to 280-fold and allows for the use of working concentrations as low as 100 pM enzyme. DNA-functionalized beta-galactosidase retains its ability to catalyze the hydrolysis of beta-glycosidic linkages once endocytosed, whereas equal concentrations of protein show little to no intracellular catalytic activity.
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