Gómez González, JacoboPeña Gil, DiegoBarka, GhofraneSciortino, GiuseppeMaréchal, Jean-DidierVázquez López, MiguelVázquez Sentís, Marco Eugenio2020-05-292020-05-292018Gómez-González J, Peña DG, Barka G, Sciortino G, Maréchal J-D, Vázquez López M and Vázquez ME (2018) Directed Self-Assembly of Trimeric DNA-Bindingchiral Miniprotein Helicates. Front. Chem. 6:520. doi: 10.3389/fchem.2018.00520http://hdl.handle.net/10347/22701We 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 DNAengCopyright © 2018 Gómez-González, Peña, Barka, Sciortino, Maréchal, Vázquez López and Vázquez. This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) and the copyright owner(s) are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these termshttp://creativecommons.org/licenses/by/4.0/MetallopeptideSelf-assembly waterDNA recognitionEnantioselectivityPeptide motifsCoordination chemistryDirected self-assembly of trimeric DNA-bindingchiral miniprotein helicatesjournal article10.3389/fchem.2018.005202296-2646open access