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Dynamics at a Peptide-TiO2 Anatase (101) Interface.

TitoloDynamics at a Peptide-TiO2 Anatase (101) Interface.
Tipo di pubblicazioneArticolo su Rivista peer-reviewed
Anno di Pubblicazione2017
AutoriPolimeni, Marco, Petridis Loukas, Smith Jeremy C., and Arcangeli Caterina
RivistaJ Phys Chem B
Volume121
Issue38
Paginazione8869-8877
Data di pubblicazione2017 Sep 28
ISSN15205207
Abstract

The interface between biological matter and inorganic materials is a widely investigated research topic due to possible applications in biomedicine and nanotechnology. In this context, the molecular level adsorption mechanism that drives specific recognition between small peptide sequences and inorganic surfaces represents an important topic likely to provide much information useful for designing bioderived materials. Here, we investigate the dynamics at the interface between a Ti-binding peptide sequence (AMRKLPDAPGMHC) and a TiO2 anatase surface by using molecular dynamics (MD) simulations. In the simulations the adsorption mechanism is characterized by diffusion of the peptide from the bulk water phase toward the TiO2 surface, followed by the anchoring of the peptide to the surface. The anchoring is mediated by the interfacial water layers by means of the charged groups of the side chains of the peptide. The peptide samples anchored and dissociated states from the surface and its conformation is not affected by the surface when anchored.

DOI10.1021/acs.jpcb.7b04707
Alternate JournalJ Phys Chem B
Citation Key6233
PubMed ID28851213