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Title: Protein-directed self-assembly of a fullerene crystal

Journal Article · · Nature Communications
DOI:https://doi.org/10.1038/ncomms11429· OSTI ID:1251209
 [1];  [2];  [1];  [1];  [3];  [4];  [5];  [3];  [6];  [7];  [8]
  1. Sungkyunkwan Univ., Suwon (Korea)
  2. New Jersey Inst. of Technology, Newark, NJ (United States)
  3. National Inst. of Science Education and Research, Odisha (India)
  4. Univ. of California, San Francisco, CA (United States); Univ. of Pennsylvania, Philadelphia, PA (United States)
  5. Univ. of Pennsylvania, Philadelphia, PA (United States)
  6. Univ. of California, San Francisco, CA (United States)
  7. Sungkyunkwan Univ., Suwon (Korea); Inst. for Basic Science (IBS), Suwon (Korea)
  8. Dartmouth College, Hanover, NH (United States)

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.

Research Organization:
Argonne National Laboratory (ANL), Argonne, IL (United States)
Sponsoring Organization:
National Science Foundation (NSF); National Institutes of Health (NIH); National Research Foundation of Korea (NRF); National Inst. of Science Education and Research; New Jersey Inst. of Technology
Grant/Contract Number:
GM54616; CHE-1413295; DMR 1120901; NRF-2014R1A1A2055647; NRF-2015M3C1A3002152; IBS-R015-D1
OSTI ID:
1251209
Journal Information:
Nature Communications, Vol. 7, Issue 1; ISSN 2041-1723
Publisher:
Nature Publishing GroupCopyright Statement
Country of Publication:
United States
Language:
ENGLISH
Citation Metrics:
Cited by: 46 works
Citation information provided by
Web of Science

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Spectroscopic and metal binding properties of a de novo metalloprotein binding a tetrazinc cluster: Chino et al. journal September 2018
Antimicrobial activity of a porphyrin binding peptide journal July 2018
General lack of structural characterization of chemically synthesized long peptides journal March 2019
Protein crystal based materials for nanoscale applications in medicine and biotechnology journal November 2018
Hierarchical design of artificial proteins and complexes toward synthetic structural biology journal December 2017
Computer Simulation of Protein Materials at Multiple Length Scales: From Single Proteins to Protein Assemblies journal January 2019
Proteins as supramolecular hosts for C 60 : a true solution of C 60 in water journal January 2018
Engineered assembly of a protein–cucurbituril biohybrid journal January 2020
Design of self-assembling transmembrane helical bundles to elucidate principles required for membrane protein folding and ion transport journal June 2017
The Immobilization of Oxindole Derivatives with Use of Cube Rhombellane Homeomorphs journal July 2019
The Immobilization of ChEMBL474807 Molecules Using Different Classes of Nanostructures journal August 2019
Docking of Polyethylenimines Derivatives on Cube Rhombellane Functionalized Homeomorphs journal August 2019
Protein Dimerization on a Phosphonated Calix[6]arene Disc journal April 2017
Exploring the Inhibitory and Antioxidant Effects of Fullerene and Fullerenol on Ribonuclease A journal September 2018