Directed Self-Assembly of Trimeric DNA-Bindingchiral Miniprotein Helicates

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...

Full description

Saved in:
Bibliographic Details
Published in:Frontiers in chemistry 2018-10, Vol.6, p.520-520
Main Authors: Gómez-González, Jacobo, Peña, Diego G, Barka, Ghofrane, Sciortino, Giuseppe, Maréchal, Jean-Didier, Vázquez López, Miguel, Vázquez, M Eugenio
Format: Article
Language:English
Subjects:
Chemistry
coordination chemistry
DNA recognition
enantioselectivity
metallopeptide
peptide motifs
self-assembly water
Citations: Items that this one cites
Items that cite this one
Online Access:Get full text
Tags: Add Tag
No Tags, Be the first to tag this record!
Description
Summary: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.
ISSN:2296-2646
2296-2646
DOI:10.3389/fchem.2018.00520