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    Probing nano-patterned peptide self-organisation at the aqueous graphene interface

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    hughes_walsh_2018.pdf (1.219Mb)
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    Publication date
    2018-01-07
    Author
    Hughes, Zak E.
    Walsh, T.R.
    Keyword
    Nanotechnology
    Graphene
    Biotechnology
    Rights
    © 2018 Royal Society of Chemistry. Full-text reproduced in accordance with the publisher’s self-archiving policy.
    Peer-Reviewed
    Yes
    
    Metadata
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    Abstract
    The peptide sequence GrBP5, IMVTESSDYSSY, is found experimentally to bind to graphene, and ex situ atomic force microscopy indicates the formation of an ordered over-layer on graphite. However, under aqueous conditions neither the molecular conformations of the adsorbed peptide chains, nor the molecular-level spatial ordering of the over-layer, has been directly resolved. Here, we use advanced molecular dynamics simulations of GrBP5, and related mutant sequences, to elucidate the adsorbed structures of both the peptide and the adsorbed peptide over-layer at the aqueous graphene interface. In agreement with a previous hypothesis, we find GrBP5 binds at the aqueous graphene interface chiefly via the tyrosine-rich C-terminal region. Our simulations of the adsorbed peptide over-layers reveal that the peptide chains form an aggregate that does not evolve further into ordered patterns. Instead, we find that the inter-chain interactions are driven by hydrogen bonding and charge–charge interactions that are not sufficiently specific to support pattern formation. Overall, we suggest that the experimentally-observed over-layer pattern may be due to the drying of the sample, and may not be prevalent at the solvated interface. However, our simulations indicate sequence modifications of GrBP5 to promote over-layer ordering under aqueous conditions.
    URI
    http://hdl.handle.net/10454/15725
    Version
    Accepted manuscript
    Citation
    Hughes ZE and Walsh TR (2018) Probing nano-patterned peptide self-organisation at the aqueous graphene interface, Nanoscale. 10(1): 302-311.
    Link to publisher’s version
    http://dx.doi.org/10.1039/c7nr06441a
    Type
    Article
    Collections
    Life Sciences Publications

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