Issue 3, 2015

Water driven adsorption of amino acids on the (101) anatase TiO2 surface: an ab initio study

Abstract

Arg, Lys and Asp amino acids are known to play a critical role in the adhesion of the RKLPDA engineered peptide on the (101) surface of the titania anatase phase. To understand their contribution to peptide adhesion, we have considered the relevant charge states due to protonation (Arg and Lys) or deprotonation (Asp) occurring in neutral water solution, and studied their adsorption on the (101) anatase TiO2 surface by ab initio total energy calculations based on density functional theory. The adsorption configurations on the hydrated surface are compared to those on the dry surface considering also the presence of the hydration shell around amino acid side-chains. This study explains how water molecules mediate the adsorption of charged amino acids showing that protonated amino acids are chemically adsorbed much more strongly than de-protonated Asp. Moreover it is shown that the polar screening of the hydration shell reduces the adsorption energy of the protonated amino acids to a small extent, thus evidencing that both Arg and Lys strongly adhere on the (101) anatase TiO2 surface in neutral water solution and that they play a major role in the adhesion of the RKLPDA peptide.

Graphical abstract: Water driven adsorption of amino acids on the (101) anatase TiO2 surface: an ab initio study

Supplementary files

Article information

Article type
Communication
Submitted
11 Jul 2014
Accepted
24 Nov 2014
First published
24 Nov 2014

Phys. Chem. Chem. Phys., 2015,17, 1556-1561

Author version available

Water driven adsorption of amino acids on the (101) anatase TiO2 surface: an ab initio study

L. Agosta, G. Zollo, C. Arcangeli, F. Buonocore, F. Gala and M. Celino, Phys. Chem. Chem. Phys., 2015, 17, 1556 DOI: 10.1039/C4CP03056G

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