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    Binding affinities of amino acid analogues at the charged aqueous titania interface: implications for titania-binding peptides

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    Publication date
    2014-11
    Author
    Sultan, A.M.
    Hughes, Zak E.
    Walsh, T.R.
    Keyword
    Titanium
    Titanium dioxide
    Water
    Peptides
    Amino acids
    Peer-Reviewed
    Yes
    
    Metadata
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    Abstract
    Despite the extensive utilization of biomolecule-titania interfaces, biomolecular recognition and interactions at the aqueous titania interface remain far from being fully understood. Here, atomistic molecular dynamics simulations, in partnership with metadynamics, are used to calculate the free energy of adsorption of different amino acid side chain analogues at the negatively-charged aqueous rutile TiO2 (110) interface, under conditions corresponding with neutral pH. Our calculations predict that charged amino acid analogues have a relatively high affinity to the titania surface, with the arginine analogue predicted to be the strongest binder. Interactions between uncharged amino acid analogues and titania are found to be repulsive or weak at best. All of the residues that bound to the negatively-charged interface show a relatively stronger adsorption compared with the charge-neutral interface, including the negatively-charged analogue. Of the analogues that are found to bind to the titania surface, the rank ordering of the binding affinities is predicted to be "arginine" > "lysine" ≈ aspartic acid > "serine". This is the same ordering as was found previously for the charge-neutral aqueous titania interface. Our results show very good agreement with available experimental data and can provide a baseline for the interpretation of peptide-TiO2 adsorption data.
    URI
    http://hdl.handle.net/10454/16953
    Version
    No full-text in the repository
    Citation
    Sultan AM, Hughes ZE and Walsh TR (2014) Binding affinities of amino acid analogues at the charged aqueous titania interface: implications for titania-binding peptides. Langmuir. 30(44): 13321-13329.
    Link to publisher’s version
    https://doi.org/10.1021/la503312d
    Type
    Article
    Collections
    Life Sciences Publications

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