DNA-Mediated Cellular Delivery of Functional Enzymes.

Autor:	Brodin JD; International Institute of Nanotechnology, ‡Department of Chemistry, and §Department of Biomedical Engineering, Northwestern University , 2145 Sheridan Road, Evanston, Illinois 60208, United States., Sprangers AJ; International Institute of Nanotechnology, ‡Department of Chemistry, and §Department of Biomedical Engineering, Northwestern University , 2145 Sheridan Road, Evanston, Illinois 60208, United States., McMillan JR; International Institute of Nanotechnology, ‡Department of Chemistry, and §Department of Biomedical Engineering, Northwestern University , 2145 Sheridan Road, Evanston, Illinois 60208, United States., Mirkin CA; International Institute of Nanotechnology, ‡Department of Chemistry, and §Department of Biomedical Engineering, Northwestern University , 2145 Sheridan Road, Evanston, Illinois 60208, United States.
Jazyk:	angličtina
Zdroj:	Journal of the American Chemical Society [J Am Chem Soc] 2015 Dec 02; Vol. 137 (47), pp. 14838-41. Date of Electronic Publication: 2015 Nov 20.
DOI:	10.1021/jacs.5b09711
Abstrakt:	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 β-galactosidase, which serves as the protein core, despite the functionalization of its surface with ∼25 DNA strands. The covalent attachment of a shell of oligonucleotides to the surface of β-galactosidase enhances its cellular uptake of by up to ∼280-fold and allows for the use of working concentrations as low as 100 pM enzyme. DNA-functionalized β-galactosidase retains its ability to catalyze the hydrolysis of β-glycosidic linkages once endocytosed, whereas equal concentrations of protein show little to no intracellular catalytic activity.
Databáze:	MEDLINE
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