Dataset Information

Tunable crystalline assemblies using surface-engineered protein cages.

ABSTRACT: Assembly of nanoparticles into superlattices yields nanomaterials with novel properties. We have recently shown that engineered protein cages are excellent building blocks for the assembly of inorganic nanoparticles into highly structured hybrid materials, with unprecedented precision. In this study, we show that the protein matrix, composed of surface-charged protein cages, can be readily tuned to achieve a number of different crystalline assemblies. Simply by altering the assembly conditions, different types of crystalline structures were produced, without the need to further modify the cages. Future work can utilize these new protein scaffolds to create nanoparticle superlattices with various assembly geometries and thus tune the functionality of these hybrid materials.

SUBMITTER: Lach M

PROVIDER: S-EPMC11337932 | biostudies-literature | 2024 Sep

REPOSITORIES: biostudies-literature

ACCESS DATA

Publications

Tunable crystalline assemblies using surface-engineered protein cages.

Lach Marcel M Rütten Michael M Beck Tobias T

Protein science : a publication of the Protein Society 20240901 9

Assembly of nanoparticles into superlattices yields nanomaterials with novel properties. We have recently shown that engineered protein cages are excellent building blocks for the assembly of inorganic nanoparticles into highly structured hybrid materials, with unprecedented precision. In this study, we show that the protein matrix, composed of surface-charged protein cages, can be readily tuned to achieve a number of different crystalline assemblies. Simply by altering the assembly conditions, ...[more]

PMID: 39167037

Similar Datasets

Project description:Porous protein cages are supramolecular protein self-assemblies presenting pores that allow the access of surrounding molecules and ions into their core in order to store and transport them in biological environments. Protein cages' pores are attractive channels for the internalisation of inorganic nanoparticles and an alternative for the preparation of hybrid bioinspired nanoparticles. However, strategies based on nanoparticle transport through the pores are largely unexplored, due to the difficulty of tailoring nanoparticles that have diameters commensurate with the pores size and simultaneously displaying specific affinity to the cages' core and low non-specific binding to the cages' outer surface. We evaluated the specific internalisation of single small gold nanoparticles, 3.9 nm in diameter, into porous protein cages via affinity binding. The E2 protein cage derived from the Geobacillus stearothermophilus presents 12 pores, 6 nm in diameter, and an empty core of 13 nm in diameter. We engineered the E2 protein by site-directed mutagenesis with oligohistidine sequences exposing them into the cage's core. Dynamic light scattering and electron microscopy analysis show that the structures of E2 protein cages mutated with bis- or penta-histidine sequences are well conserved. The surface of the gold nanoparticles was passivated with a self-assembled monolayer made of a mixture of short peptidols and thiolated alkane ethylene glycol ligands. Such monolayers are found to provide thin coatings preventing non-specific binding to proteins. Further functionalisation of the peptide coated gold nanoparticles with Ni2+ nitrilotriacetic moieties enabled the specific binding to oligohistidine tagged cages. The internalisation via affinity binding was evaluated by electron microscopy analysis. From the various mutations tested, only the penta-histidine mutated E2 protein cage showed repeatable and stable internalisation. The present work overcomes the limitations of currently available approaches and provides a new route to design tailored and well-controlled hybrid nanoparticles.

Dataset Information

Tunable crystalline assemblies using surface-engineered protein cages.

Publications

Tunable crystalline assemblies using surface-engineered protein cages.

Similar Datasets

OmicsDI is part of the ELIXIR infrastructure

Tweets