Jump to main content
Jump to site search

Issue 6, 2020
Previous Article Next Article

Protein-directed crystalline 2D fullerene assemblies

Author affiliations

Abstract

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.

Graphical abstract: Protein-directed crystalline 2D fullerene assemblies

Back to tab navigation

Supplementary files

Article information


Submitted
16 Aug 2019
Accepted
05 Nov 2019
First published
08 Jan 2020

This article is Open Access

Nanoscale, 2020,12, 3614-3622
Article type
Communication

Protein-directed crystalline 2D fullerene assemblies

M. Liutkus, A. López-Andarias, S. H. Mejías, J. López-Andarias, D. Gil-Carton, F. Feixas, S. Osuna, W. Matsuda, T. Sakurai, S. Seki, C. Atienza, N. Martín and A. L. Cortajarena, Nanoscale, 2020, 12, 3614
DOI: 10.1039/C9NR07083D

This article is licensed under a Creative Commons Attribution-NonCommercial 3.0 Unported Licence. Material from this article can be used in other publications provided that the correct acknowledgement is given with the reproduced material and it is not used for commercial purposes.

Reproduced material should be attributed as follows:

  • For reproduction of material from NJC:
    [Original citation] - Published by The Royal Society of Chemistry (RSC) on behalf of the Centre National de la Recherche Scientifique (CNRS) and the RSC.
  • For reproduction of material from PCCP:
    [Original citation] - Published by the PCCP Owner Societies.
  • For reproduction of material from PPS:
    [Original citation] - Published by The Royal Society of Chemistry (RSC) on behalf of the European Society for Photobiology, the European Photochemistry Association, and RSC.
  • For reproduction of material from all other RSC journals:
    [Original citation] - Published by The Royal Society of Chemistry.

Information about reproducing material from RSC articles with different licences is available on our Permission Requests page.


Social activity

Search articles by author

Spotlight

Advertisements