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2015 MRS Spring Meeting


GG3.07 - Atomistic Simulations of Proteins Interacting with Gold Surfaces and Nanoparticles


Apr 8, 2015 10:30am ‐ Apr 8, 2015 11:00am

Description

The interface between proteins and, extended or nanostructured, inorganic surfaces, is the key element of several current and potential biotechnological applications. For example, redox enzymes may be supported on electrodes, to create biofuel cells able to use fuel other than hydrogen [1]; peptides able to specifically bind a given surface have the potential to guide the self-assembling of nanosystems [2]. In a more biologically-oriented context, the interaction of amyloidogenic proteins with surfaces and nanoparticles is being investigated to understand how such interaction may affect the misfolding and fibrillation process [3]. Bare and functionalized gold surfaces, and gold nanoparticles, are particularly relevant in these frameworks. Au surfaces are often used for electrodes or to support self-assembled monolayers. Au nanoparticles are relatively cheap, can be synthesized with a good control of shape, size, and functionalization, and present useful optical properties. We have developed and applied tools for the atomistic simulations of the interaction of proteins and peptides with various surfaces of gold [4,5], including functionalized ones, and with gold nanoparticles [6,7]. In this talks, such tools will be introduced and some examples of their applications relevant for material science (e.g., enzymatic biofuel cells [8]) and nanobiotechnology (e.g., interaction of gold nanoparticles with amyloidogenic proteins/peptides [7]) will be presented. [1] Cracknell, J. A. et al. Chem. Rev. 108, 2439 (2008) [2] Sarikaya, M., et al. Nature Mater. 3, 577 (2003) [3] Linse, S., et al. PNAS 104, 8691 (2007) [4] Iori, F. et al. J. Comp. Chem. 30, 1465 (2009) [5] Wright, L. et al. JCTC 9, 1616 (2013); JPC C 117, 24292 (2013) [6] Brancolini, G. et al. ACS Nano 6, 9863 (2012) [7] Brancolini, G. et al. Nanoscale 6, 7903 (2014) [8] Zanetti-Polzi, L. et al. JACS 136, 12929 (2014)

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