Dynamic Stereoselection of Peptide Helicates and Their Selective Labeling of DNA Replication Foci in Cells**

Jacobo Gómez-González, Yolanda Pérez, Giuseppe Sciortino, Lorena Roldan-Martín, José Martínez-Costas, Jean Didier Maréchal, Ignacio Alfonso, Miguel Vázquez López*, M. Eugenio Vázquez*

*Autor corresponent d’aquest treball

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27 Cites (Scopus)

Resum

Although largely overlooked in peptide engineering, coordination chemistry offers a new set of interactions that opens unexplored design opportunities for developing complex molecular structures. In this context, we report new artificial peptide ligands that fold into chiral helicates in the presence of labile metal ions such as FeII and CoII. Heterochiral β-turn-promoting sequences encode the stereoselective folding of the peptide ligands and define the physicochemical properties of their corresponding metal complexes. Circular dichroism and NMR spectroscopy in combination with computational methods allowed us to identify and determine the structure of two isochiral ΛΛ-helicates, folded as topological isomers. Finally, in addition to the in-vitro characterization of their selective binding to DNA three-way junctions, cell-microscopy experiments demonstrated that a rhodamine-labeled FeII helicate was internalized and selectively stains DNA replication factories in functional cells.

Idioma originalEnglish
Pàgines (de-a)8859-8866
Nombre de pàgines8
RevistaAngewandte Chemie - International Edition
Volum60
Número16
DOIs
Estat de la publicacióPublicada - 12 d’abr. 2021

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