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Enzymatic activation of cell-penetrating peptides in self-assembled nanostructures triggers fibre-to-micelle morphological transition

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Abstract

We report here a proof-of-concept design of a multi-domain cell-penetrating peptide amphiphile (CPPA) which can self-assemble into fibrous nanostructures and transform into spherical micelles upon enzymatic degradation by matrix metalloproteinase-2 (MMP-2) up-regulated in the tumour environment. Concomitant with this morphological transition, the cell-penetrating peptide (CPP), which was previously buried inside the CPPA fibers, could be presented on the surface of the CPPA micelles, enhancing their cell-penetrating ability. These multifunctional and enzyme-responsive CPP nanostructures hold potential as nanocarriers for tumour-targeted intracellular delivery of therapeutic and diagnostic agents.

Graphical abstract: Enzymatic activation of cell-penetrating peptides in self-assembled nanostructures triggers fibre-to-micelle morphological transition

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Publication details

The article was received on 08 May 2017, accepted on 07 Jun 2017 and first published on 07 Jun 2017


Article type: Communication
DOI: 10.1039/C7CC03512H
Citation: Chem. Commun., 2017, Advance Article
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    Enzymatic activation of cell-penetrating peptides in self-assembled nanostructures triggers fibre-to-micelle morphological transition

    Y. Shi, Y. Hu, G. Ochbaum, R. Lin, R. Bitton, H. Cui and H. S. Azevedo, Chem. Commun., 2017, Advance Article , DOI: 10.1039/C7CC03512H

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