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Coiled‐Coil‐Mediated Activation of Oligoarginine Cell‐Penetrating Peptides
Author(s) -
Bode Saskia A.,
Kruis Ilmar C.,
Adams Hans P. J. H. M.,
Boelens Wilbert C.,
Pruijn Ger J. M.,
van Hest Jan C. M.,
Löwik Dennis W. P. M.
Publication year - 2017
Publication title -
chembiochem
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.05
H-Index - 126
eISSN - 1439-7633
pISSN - 1439-4227
DOI - 10.1002/cbic.201600614
Subject(s) - coiled coil , chemistry , cell , biophysics , microbiology and biotechnology , biochemistry , nanotechnology , materials science , biology
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.