Proteins are hetero-polymers made-up of single building blocks (aminoacids) whose composition determines folding and final architecture. Some proteins are able to undergo self-assembly process enabling the formation of ordered molecular aggregates that in some cases assume conformations particularly suitable to nanotechnological applications. In this work we describe the properties of a ring-like decameric protein, Peroxiredoxin (Prx), to build composite materials interacting with or catalyzing the formation of selectively metal nanoparticles that can be trapped over the surface of nanostructured graphene oxide (GO) sheets. We demonstrate furthermore the ability of Prx to guide the formation of 3D layers of GO embedding metal nanoparticles in the composite material. These composites are discussed as possible precursors to electronic and chemical devices.

Protein-Based Nanostructures and Their Self-assembly with Graphene Oxide

Ippoliti, R.;Ardini, M.;Di Leandro, L.;Giansanti, F.;Cimini, A.;Ottaviano, L.;Angelucci, F.
2017-01-01

Abstract

Proteins are hetero-polymers made-up of single building blocks (aminoacids) whose composition determines folding and final architecture. Some proteins are able to undergo self-assembly process enabling the formation of ordered molecular aggregates that in some cases assume conformations particularly suitable to nanotechnological applications. In this work we describe the properties of a ring-like decameric protein, Peroxiredoxin (Prx), to build composite materials interacting with or catalyzing the formation of selectively metal nanoparticles that can be trapped over the surface of nanostructured graphene oxide (GO) sheets. We demonstrate furthermore the ability of Prx to guide the formation of 3D layers of GO embedding metal nanoparticles in the composite material. These composites are discussed as possible precursors to electronic and chemical devices.
978-3-319-58132-3
978-3-319-58134-7
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Utilizza questo identificativo per citare o creare un link a questo documento: https://hdl.handle.net/11697/140696
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