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Angew Chem Int Ed Engl. 2015 Sep 1;54(36):10583-6. doi: 10.1002/anie.201505437. Epub 2015 Jul 31.

Protein Delivery System Containing a Nickel-Immobilized Polymer for Multimerization of Affinity-Purified His-Tagged Proteins Enhances Cytosolic Transfer.

Author information

1
UMR 7199 and UMR 7213 CNRS Université de Strasbourg, Faculté de Pharmacie, Illkirch (France).
2
UMR 7242, Ecole supérieure de biotechnologie Strasbourg, Illkirch (France).
3
Centre for Integrative Biology (CBI), IGBMC, Illkirch (France).
4
UMR 7199 and UMR 7213 CNRS Université de Strasbourg, Faculté de Pharmacie, Illkirch (France). zuber@unistra.fr.

Abstract

Recombinant proteins with cytosolic or nuclear activities are emerging as tools for interfering with cellular functions. Because such tools rely on vehicles for crossing the plasma membrane we developed a protein delivery system consisting in the assembly of pyridylthiourea-grafted polyethylenimine (πPEI) with affinity-purified His-tagged proteins pre-organized onto a nickel-immobilized polymeric guide. The guide was prepared by functionalization of an ornithine polymer with nitrilotriacetic acid groups and shown to bind several His-tagged proteins. Superstructures were visualized by electron and atomic force microscopy using 2 nm His-tagged gold nanoparticles as probes. The whole system efficiently carried the green fluorescent protein, single-chain antibodies or caspase 3, into the cytosol of living cells. Transduction of the protease caspase 3 induced apoptosis in two cancer cell lines, demonstrating that this new protein delivery method could be used to interfere with cellular functions.

KEYWORDS:

drug delivery; nanocarriers; protein delivery; proteins; self-assembly

PMID:
26230624
DOI:
10.1002/anie.201505437
[Indexed for MEDLINE]

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