Thiolated Lysine-Leucine Peptides Self-Assemble into Biosilica Nucleation Pits on Gold Surfaces

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

  • Hao Lu, Max-Planck Institute for Polymer Research, Mainz, Tyskland
  • Yeneneh Yimer, Department of Chemical Engineering, University of Washington, Seattle, WA 98195, USA., USA
  • Ruediger Berger, Max-Planck Institute for Polymer Research, Mainz, Tyskland
  • Mischa Bonn, Max-Planck Institute for Polymer Research, Mainz, Tyskland
  • Jim Pfaendtner, Department of Chemical Engineering, University of Washington, Seattle, WA 98195, USA., USA
  • Tobias Weidner

Nanostructured silica architectures have led to many applications in electronic and optical devices, and catalysis. Recently, bioinspired approaches based on peptide-assisted silica fabrication have attracted great attention because of low production cost and mild, sustainable fabrication methods. Herein it is demonstrated that biomimetic peptides can also exert control over silica mineralization when bounded to inorganic surfaces. The amphiphilic alpha-helical peptide LK alpha 14 (Ac-LKKLLKLLKKLLKLC-OH) is used, which is based on leucine and lysine and has been a model system for surface studies and mineralization in solution for several years. LK alpha 14 has been anchored to gold surfaces via terminal cysteine groups as linkers. Using X-ray photoelectron spectroscopy, vibrational sum frequency generation spectroscopy, scanning force microscopy, and molecular dynamic simulations, it is found that LK alpha 14 peptides assemble into laterally ordered structures with approximate to 5 nm wide cavities which serve as effective nucleating sites for silica nanoparticles.

OriginalsprogEngelsk
Artikelnummer1700399
TidsskriftAdvanced Materials Interfaces
Vol/bind4
Nummer16
Sider (fra-til)1700399, 1-7
Antal sider7
ISSN2196-7350
DOI
StatusUdgivet - 2017

Se relationer på Aarhus Universitet Citationsformater

ID: 118014046