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Directed Self-Assembly of Trimeric DNA-Bindingchiral Miniprotein Helicates.

ABSTRACT: 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.

SUBMITTER: Gomez-Gonzalez J

PROVIDER: S-EPMC6218460 | biostudies-literature | 2018

REPOSITORIES: biostudies-literature

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Directed Self-Assembly of Trimeric DNA-Bindingchiral Miniprotein Helicates.

Gómez-González Jacobo J Peña Diego G DG Barka Ghofrane G Sciortino Giuseppe G Maréchal Jean-Didier JD Vázquez López Miguel M Vázquez M Eugenio ME

Frontiers in chemistry 20181030

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 ...[more]

PMID: 30425980

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