Reversible activation of pH-sensitive cell penetrating peptides attached to gold surfaces

  • Chem Commun (Camb). 2015;51(2):273-275. doi: 10.1039/c4cc07278b.
Joe E Baio  #  1 ,  Denise Schach  #  1 ,  Adrian V Fuchs  1 ,  Lars Schmüser  1 ,  Nils Billecke  1 ,  Christoph Bubeck  1 ,  Katharina Landfester  1 ,  Mischa Bonn  1 ,  Michael Bruns  2 ,  Clemens K Weiss  1  3 ,  Tobias Weidner  1
Affiliations
  • 1. Max Planck Institute for Polymer Research, 55270 Mainz, Germany.
  • 2. Karlsruhe Institute of Technology, Institute for Applied Materials and Karlsruhe Nano Micro Facility, 76344 Eggenstein-Leopoldshafen, Germany.
  • 3. University of Applies Sciences Bingen, 55411 Bingen, Germany.
  • # Contributed equally.
PMID: 25329926 DOI: 10.1039/c4cc07278b
Abstract

pH-sensitive viral fusion protein mimics are widely touted as a promising route towards site-specific delivery of therapeutic compounds across lipid membranes. Here, we demonstrate that a fusion protein mimic, designed to achieve a reversible, pH-driven helix-coil transition mechanism, retains its functionality when covalently bound to a surface.

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