Directed self-assembly of trimeric DNA-bindingchiral miniprotein helicates

Jacobo Gómez-González, Diego G. Peña, Ghofrane Barka, Giuseppe Sciortino, Jean Didier Maréchal, Miguel Vázquez López, M. Eugenio Vázquez

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8 Citations (Scopus)


© 2018 Gómez-González, Peña, Barka, Sciortino, Maréchal, Vázquez López and Vázquez. We propose that peptides are highly versatile platforms for the precise design of supramolecular metal architectures, and particularly, for the controlled assembly of helicates. In this context, we show that the bacteriophage T4 Fibritin foldon (T4Ff) can been engineered on its N-terminus with metal-chelating 2,2'-bipyridine units that stereoselectively assemble in the presence of Fe(II) into parallel, three-stranded peptide helicates with preferred helical orientation. Modeling studies support the proposed self-assembly and the stability of the final helicate. Furthermore, we show that these designed mini-metalloproteins selectively recognize three-way DNA junctions over double-stranded DNA.
Original languageEnglish
Article number520
JournalFrontiers in Chemistry
Publication statusPublished - 1 Oct 2018


  • Coordination chemistry
  • DNA recognition
  • Enantioselectivity
  • Metallopeptide
  • Peptide motifs
  • Self-assembly water


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