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Protein-directed self-assembly of a fullerene crystal

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Title
Protein-directed self-assembly of a fullerene crystal
Author(s)
Kook-Han Kim; Dong-Kyun Ko; Yong-Tae Kim; Nam Hyeong Kim; Jaydeep Paul; Shao-Qing Zhang; Christopher B. Murray; Rudresh Acharya; William F. DeGrado; Yong Ho Kim; Gevorg Grigoryan
Publication Date
2016-04
Journal
NATURE COMMUNICATIONS, v.7, no., pp.11429 -
Publisher
NATURE PUBLISHING GROUP
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 (C 60) into ordered superstructures. A previously engineered tetrameric helical bundle binds C 60 in solution, rendering it water soluble. Two tetramers associate with one C 60, 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 C 60 are electrically insulating. The affinity of C 60 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
URI
http://pr.ibs.re.kr/handle/8788114/2540
ISSN
2041-1723
Appears in Collections:
Center for Neuroscience Imaging Research (뇌과학 이미징 연구단) > Journal Papers (저널논문)
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