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Protein-directed self-assembly of a fullerene crystal.

  • Author(s): Kim, Kook-Han
  • Ko, Dong-Kyun
  • Kim, Yong-Tae
  • Kim, Nam Hyeong
  • Paul, Jaydeep
  • Zhang, Shao-Qing
  • Murray, Christopher B
  • Acharya, Rudresh
  • DeGrado, William F
  • Kim, Yong Ho
  • Grigoryan, Gevorg
  • et al.
Abstract

Learning to engineer self-assembly would enable the precise organization of molecules by design to create matter with tailored properties. Here we demonstrate that proteins can direct the self-assembly of buckminsterfullerene (C60) into ordered superstructures. A previously engineered tetrameric helical bundle binds C60 in solution, rendering it water soluble. Two tetramers associate with one C60, promoting further organization revealed in a 1.67-Å crystal structure. Fullerene groups occupy periodic lattice sites, sandwiched between two Tyr residues from adjacent tetramers. Strikingly, the assembly exhibits high charge conductance, whereas both the protein-alone crystal and amorphous C60 are electrically insulating. The affinity of C60 for its crystal-binding site is estimated to be in the nanomolar range, with lattices of known protein crystals geometrically compatible with incorporating the motif. Taken together, these findings suggest a new means of organizing fullerene molecules into a rich variety of lattices to generate new properties by design.

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