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
Source abstract
Abstract
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.
Source: openalex_inverted_index · Quality: baseline
Research context
OpenAlex topics: Block Copolymer Self-Assembly · Pickering emulsions and particle stabilization · Catalysis for Biomass Conversion
SciVX discovery tags are terminology-based. OpenAlex topics are source-provided classifications.
Affiliations
Univ. Grenoble Alpes, CNRS, CEA, INRAE, IRIG-DBSCI-LPCV, 38000 Grenoble, France
Univ. Grenoble Alpes, CEA, CNRS, IRIG-DIESE-SYMMES, 38000 Grenoble, France
Univ. Grenoble Alpes, CEA, CNRS, IRIG-DIESE-MEM, 38000 Grenoble, France
Univ. Grenoble Alpes, CEA, LETI, MINATEC Campus, 38000 Grenoble, France
Funding
Labex · Commissariat ?? l'??nergie Atomique et aux ??nergies Alternatives · LabEx Grenoble Alliance for Cell and Structural Biology · CBH-EUR-GS · CEA Nanoprot 3D
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