Acetylation dictates the morphology of nanophase biosilica precipitated by a 14-amino acid leucine-lysine peptide

Publikation: Bidrag til tidsskrift/Konferencebidrag i tidsskrift /Bidrag til avisTidsskriftartikelForskningpeer review


  • Helmut Lutz, Max Planck Institute for Polymer Research
  • ,
  • Vance Jaeger, University of Washington, Seattle
  • ,
  • Mischa Bonn, Max Planck Institute for Polymer Research
  • ,
  • Jim Pfaendtner, University of Washington, Seattle
  • ,
  • Tobias Weidner

N-terminal acetylation is a commonly used modification technique for synthetic peptides, mostly applied for reasons of enhanced stability, and in many cases regarded as inconsequential. In engineered biosilification - the controlled deposition of silica for nanotechnology applications by designed peptides - charged groups often play a deciding role. Here we report that changing the charge by acetylation of a 14-amino acid leucine-lysine (LK) peptide dramatically changes the morphology of precipitated biosilica; acetylated LK peptides produce nano-spheres, whereas nano-wires are precipitated by the same peptide in a non-acetylated form. By using interface-specific vibrational spectroscopy and coarse-grained molecular simulations, we show that this change in morphology is not the result of modified peptide-silica interactions, but rather caused by the stabilization of the hydrophobic core of peptide aggregates created by the removal of a peptide charge upon acetylation. These results should raise awareness of the potential impact of N-terminal modifications in peptide applications.

TidsskriftJournal of Peptide Science
Sider (fra-til)141-147
Antal sider7
StatusUdgivet - 2017

Se relationer på Aarhus Universitet Citationsformater

ID: 108449455