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Chembiochem. 2017 Jan 17;18(2):185-188. doi: 10.1002/cbic.201600614. Epub 2016 Dec 14.

Coiled-Coil-Mediated Activation of Oligoarginine Cell-Penetrating Peptides.

Author information

1
Bio-Organic Chemistry, Radboud University Nijmegen, Heyendaalseweg 135, 6525 AJ, Nijmegen, Netherlands.
2
Biomolecular Chemistry, Radboud University Nijmegen, Heyendaalseweg 135, 6525 AJ, Nijmegen, Netherlands.

Abstract

A supramolecular approach was undertaken to create functionally activatable cell-penetrating peptides. Two tetra-arginines were assembled into an active cell-penetrating peptide by heterodimerizing leucine zippers. Three different leucine-zipper pairs were evaluated: activation was found to depend on the association constant of the coiled-coil peptides. The weaker-binding peptides required an additional disulfide linkage to induce cell-penetrating capability, whereas for the most-stable coiled-coil no additional stabilization was needed. The latter zipper pair was used to show that the induced formation of the coiled coils allows control over the uptake of an oligoarginine CPP-conjugated cargo protein.

KEYWORDS:

activatable cellular uptake; cell-penetrating peptides; drug delivery; fluorescent probes; leucine zippers; noncovalent conjugation

PMID:
27870530
DOI:
10.1002/cbic.201600614
[Indexed for MEDLINE]

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