DNA-Mediated Cellular Delivery of Functional Enzymes

Jeffrey D. Brodin, Anthony J. Sprangers, Janet R. McMillan, Chad A. Mirkin*

*Corresponding author for this work

Research output: Contribution to journalArticle

62 Scopus citations

Abstract

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.

Original languageEnglish (US)
Pages (from-to)14838-14841
Number of pages4
JournalJournal of the American Chemical Society
Volume137
Issue number47
DOIs
StatePublished - Nov 20 2015

ASJC Scopus subject areas

  • Catalysis
  • Chemistry(all)
  • Biochemistry
  • Colloid and Surface Chemistry

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