Water soluble 2D crystalline monolayers of fullerenes grow on planar assemblies of engineered consensus tetratricopeptide repeat proteins. Designed fullerene-coordinating tyrosine clamps on the protein introduce specific fullerene binding sites, which facilitate fullerene nucleation. Through reciprocal interactions between the components, the hybrid material assembles into two-dimensional 2 nm thick structures with crystalline order, that conduct photo-generated charges. Thus, the protein-fullerene hybrid material is a demonstration of the developments toward functional materials with protein-based precision control of functional elements.
CITATION STYLE
Liutkus, M., López-Andarias, A., Mejías, S. H., López-Andarias, J., Gil-Carton, D., Feixas, F., … Cortajarena, A. L. (2020). Protein-directed crystalline 2D fullerene assemblies. Nanoscale, 12(6), 3614–3622. https://doi.org/10.1039/c9nr07083d
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