Nanoscale dynamics and protein adhesivity of alkylamine self-assembled monolayers on graphene

Show simple item record O'Mahony, Shane O'Dwyer, Colm Nijhuis, C. A. Greer, James C. Quinn, Aidan J. Thompson, Damien 2018-05-17T15:43:40Z 2018-05-17T15:43:40Z 2013-01-09
dc.identifier.citation O’Mahony, S., O’Dwyer, C., Nijhuis, C. A., Greer, J. C., Quinn, A. J. and Thompson, D. (2013) 'Nanoscale Dynamics and Protein Adhesivity of Alkylamine Self-Assembled Monolayers on Graphene', Langmuir, 29(24), pp. 7271-7282. doi: 10.1021/la304545n en
dc.identifier.volume 29 en
dc.identifier.startpage 7271 en
dc.identifier.endpage 7282 en
dc.identifier.issn 0743-7463
dc.identifier.doi 10.1021/la304545n
dc.description.abstract Atomic-scale molecular dynamics computer simulations are used to probe the structure, dynamics, and energetics of alkylamine self-assembled monolayer (SAM) films on graphene and to model the formation of molecular bilayers and protein complexes on the films. Routes toward the development and exploitation of functionalized graphene structures are detailed here, and we show that the SAM architecture can be tailored for use in emerging applications (e.g., electrically stimulated nerve fiber growth via the targeted binding of specific cell surface peptide sequences on the functionalized graphene scaffold). The simulations quantify the changes in film physisorption on graphene and the alkyl chain packing efficiency as the film surface is made more polar by changing the terminal groups from methyl (−CH3) to amine (−NH2) to hydroxyl (−OH). The mode of molecule packing dictates the orientation and spacing between terminal groups on the surface of the SAM, which determines the way in which successive layers build up on the surface, whether via the formation of bilayers of the molecule or the immobilization of other (macro)molecules (e.g., proteins) on the SAM. The simulations show the formation of ordered, stable assemblies of monolayers and bilayers of decylamine-based molecules on graphene. These films can serve as protein adsorption platforms, with a hydrophobin protein showing strong and selective adsorption by binding via its hydrophobic patch to methyl-terminated films and binding to amine-terminated films using its more hydrophilic surface regions. Design rules obtained from modeling the atomic-scale structure of the films and interfaces may provide input into experiments for the rational design of assemblies in which the electronic, physicochemical, and mechanical properties of the substrate, film, and protein layer can be tuned to provide the desired functionality. en
dc.description.sponsorship National Research Foundation Singapore (NRF-CRP 8-2011-07) en
dc.format.mimetype application/pdf en
dc.language.iso en en
dc.publisher American Chemical Society (ACS) en
dc.rights © 2013 American Chemical Society. This document is the Accepted Manuscript version of a Published Work that appeared in final form in Langmuir, copyright © American Chemical Society after peer review and technical editing by the publisher. To access the final edited and published work see en
dc.subject Graphene functionalization en
dc.subject Self-assembly en
dc.subject Bilayers en
dc.subject Alkylamine en
dc.subject Hydrophobin protein en
dc.subject Computer-aided design en
dc.subject Molecular dynamics en
dc.subject Nanostructured scaffolds en
dc.subject Cell immobilization en
dc.subject Molecular-dynamics en
dc.subject Surface interactions en
dc.subject Carbon nanotubes en
dc.subject Monolayers en
dc.subject Hydrophobin en
dc.subject Films en
dc.subject Recognition en
dc.subject Simulations en
dc.subject Peptide en
dc.subject Functionalization en
dc.title Nanoscale dynamics and protein adhesivity of alkylamine self-assembled monolayers on graphene en
dc.type Article (peer-reviewed) en
dc.internal.authorcontactother Colm O'Dwyer, Chemistry, University College Cork, Cork, Ireland. +353-21-490-3000 Email: en
dc.internal.availability Full text available en 2018-05-15T23:42:42Z
dc.description.version Accepted Version en
dc.internal.rssid 279269366
dc.internal.rssid 288086101
dc.internal.wokid 000320748200014
dc.contributor.funder Science Foundation Ireland en
dc.contributor.funder National Research Foundation Singapore en
dc.description.status Peer reviewed en
dc.identifier.journaltitle Langmuir en
dc.internal.copyrightchecked Yes en
dc.internal.licenseacceptance Yes en
dc.internal.IRISemailaddress en
dc.relation.project info:eu-repo/grantAgreement/SFI/SFI Starting Investigator Research Grant (SIRG)/11/SIRG/B2111/IE/Engineering Multivalent Proteins for Regenerative Medicine (EMPoRiuM)/ en

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