Tunable crystalline assemblies using surface‐engineered protein cages

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.

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Publication Details

Journal
Protein Science
Published
2024-08-21
DOI
https://doi.org/10.1002/pro.5153
Citations
2
Primary Topic
Bacteriophages and microbial interactions
Type
article
Field-Weighted Citation Impact
0.92

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article

Tunable crystalline assemblies using surface‐engineered protein cages

Michael Rütten, Marcel Lach, Tobias Beck
2 citations
Protein Science
Bacteriophages and microbial interactions
0.92
article

Tunable crystalline assemblies using surface‐engineered protein cages

Michael Rütten, Marcel Lach, Tobias Beck
article en
2 citations

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.

Protein ScienceVol. 33(9)
Universität Hamburg (DE), Hamburg Institut (Germany) (DE), Max Planck Institute for the Structure and Dynamics of Matter (DE), Hamburg Centre for Ultrafast Imaging
Fonds der Chemischen Industrie, Deutsche Forschungsgemeinschaft
Openalex Percentile: Top 23%
Bacteriophages and microbial interactions
0.92
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