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

doi:10.3389/fchem.2018.00520

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

Department of Chemistry

Research output: Contribution to journal › Article › Research

4 Citations (Scopus)

Abstract

© 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 language	English
Article number	520
Journal	Frontiers in Chemistry
Volume	6
DOIs	https://doi.org/10.3389/fchem.2018.00520
Publication status	Published - 1 Oct 2018

Keywords

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

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10.3389/fchem.2018.00520

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title = "Directed self-assembly of trimeric DNA-bindingchiral miniprotein helicates",

abstract = "{\textcopyright} 2018 G{\'o}mez-Gonz{\'a}lez, Pe{\~n}a, Barka, Sciortino, Mar{\'e}chal, V{\'a}zquez L{\'o}pez and V{\'a}zquez. 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.",

keywords = "Coordination chemistry, DNA recognition, Enantioselectivity, Metallopeptide, Peptide motifs, Self-assembly water",

author = "Jacobo G{\'o}mez-Gonz{\'a}lez and Pe{\~n}a, {Diego G.} and Ghofrane Barka and Giuseppe Sciortino and Mar{\'e}chal, {Jean Didier} and L{\'o}pez, {Miguel V{\'a}zquez} and V{\'a}zquez, {M. Eugenio}",

year = "2018",

month = oct,

day = "1",

doi = "10.3389/fchem.2018.00520",

language = "English",

volume = "6",

journal = "Frontiers in Chemistry",

issn = "2296-2646",

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TY - JOUR

T1 - Directed self-assembly of trimeric DNA-bindingchiral miniprotein helicates

AU - Gómez-González, Jacobo

AU - Peña, Diego G.

AU - Barka, Ghofrane

AU - Sciortino, Giuseppe

AU - Maréchal, Jean Didier

AU - López, Miguel Vázquez

AU - Vázquez, M. Eugenio

PY - 2018/10/1

Y1 - 2018/10/1

N2 - © 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.

AB - © 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.

KW - Coordination chemistry

KW - DNA recognition

KW - Enantioselectivity

KW - Metallopeptide

KW - Peptide motifs

KW - Self-assembly water

U2 - 10.3389/fchem.2018.00520

DO - 10.3389/fchem.2018.00520

M3 - Article

C2 - 30425980

VL - 6

JO - Frontiers in Chemistry

JF - Frontiers in Chemistry

SN - 2296-2646

M1 - 520

ER -