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

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, vol. 30, no. 44, pp. 13321-13329, doi: 10.1021/la503312d.

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Title Binding affinities of amino acid analogues at the charged aqueous titania interface : implications for titania-binding peptides
Author(s) Sultan,AM
Hughes,ZE
Walsh,TRORCID iD for Walsh,TR orcid.org/0000-0002-0233-9484
Journal name Langmuir
Volume number 30
Issue number 44
Start page 13321
End page 13329
Total pages 9
Publisher American Chemical Society
Place of publication Washington, United States
Publication date 2014-11-11
ISSN 1520-5827
Keyword(s) Science & Technology
Physical Sciences
Technology
Chemistry, Multidisciplinary
Chemistry, Physical
Materials Science, Multidisciplinary
Chemistry
Materials Science
MOLECULAR-DYNAMICS SIMULATIONS
FREE-ENERGY CALCULATIONS
ELECTRIC DOUBLE-LAYER
METAL-OXIDE SURFACES
RUTILE 110 SURFACE
LIQUID WATER
AB-INITIO
ADSORPTION
TIO2
IDENTIFICATION
Summary 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.
Language eng
DOI 10.1021/la503312d
Field of Research 030603 Colloid and Surface Chemistry
Socio Economic Objective 970110 Expanding Knowledge in Technology
HERDC Research category C1 Refereed article in a scholarly journal
Copyright notice ©2014, American Chemical Society
Persistent URL http://hdl.handle.net/10536/DRO/DU:30069081

Document type: Journal Article
Collection: Institute for Frontier Materials
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Citation counts: TR Web of Science Citation Count  Cited 11 times in TR Web of Science
Scopus Citation Count Cited 9 times in Scopus
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