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Dynamic Stereoselection of Peptide Helicates and Their Selective Labeling of DNA Replication Foci in Cells **
Author(s) -
GómezGonzález Jacobo,
Pérez Yolanda,
Sciortino Giuseppe,
RoldanMartín Lorena,
MartínezCostas José,
Maréchal JeanDidier,
Alfonso Ignacio,
Vázquez López Miguel,
Vázquez M. Eugenio
Publication year - 2021
Publication title -
angewandte chemie international edition
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.831
H-Index - 550
eISSN - 1521-3773
pISSN - 1433-7851
DOI - 10.1002/anie.202013039
Subject(s) - chemistry , peptide , context (archaeology) , dna , circular dichroism , folding (dsp implementation) , stereochemistry , dna replication , combinatorial chemistry , biochemistry , biology , paleontology , electrical engineering , engineering
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 Fe II and Co II . 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 Fe II helicate was internalized and selectively stains DNA replication factories in functional cells.