Self-Assembly of a Ginkgo Oligomerization Domain Creates a Sub-10-nm Honeycomb Architecture on Carbon and Silicon Surfaces with Customizable Pores: Implications for Nanoelectronics, Biosensing, and Biocatalysis
journal contributionposted on 09.09.2021, 11:35 by Elise Jacquier, Pierre-Henri Jouneau, Denis Falconet, Denis Mariolle, Emmanuel Thévenon, Grégory Si Larbi, Raluca Tiron, François Parcy, Pierre-Henri Elchinger, Renaud Dumas
Over the last decade, protein self-assembly techniques have been extensively studied and improved, enabling the production of a wide range of different nanometric patterns. However, most studies in this field depict thin self-assemblies of a few nanometers in height, while precise grafting of molecules on the patterns remains challenging. We present here a natural polymeric honeycomb organization based on the self-assembly abilities of a Ginkgo biloba protein oligomerization domain. This honeycomb architecture depicts 3D pores of 5 nm diameter and a height of 40 stacked proteins. Each protein has tunable N- and C-terminal extensions located inside the pore, allowing different bindings of ligands in the pore. The proof of concept is illustrated here by the distinctive metallization of the pores with nickel or gold. Overall, these characteristics make this honeycomb a versatile platform, paving the way for major biotechnological advances that were not possible with current nanomaterials.
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patterns remains challengingmajor biotechnological advancesdifferent nanometric patternsallowing different bindings5 nm diameter40 stacked proteinsnm honeycomb architecturewide rangeversatile platformtunable nsilicon surfacesprecise graftinglast decadeextensively studieddistinctive metallizationcurrent nanomaterialscharacteristics make