TY - JOUR
T1 - Dynamic Stereoselection of Peptide Helicates and Their Selective Labeling of DNA Replication Foci in Cells**
AU - Gómez-González, Jacobo
AU - Pérez, Yolanda
AU - Sciortino, Giuseppe
AU - Roldan-Martín, Lorena
AU - Martínez-Costas, José
AU - Maréchal, Jean Didier
AU - Alfonso, Ignacio
AU - Vázquez López, Miguel
AU - Vázquez, M. Eugenio
N1 - Publisher Copyright:
© 2020 Wiley-VCH GmbH
PY - 2021/4/12
Y1 - 2021/4/12
N2 - 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.
AB - 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.
KW - coordination chemistry
KW - DNA recognition
KW - metallopeptides
KW - peptide design
KW - supramolecular chemistry
UR - http://www.scopus.com/inward/record.url?scp=85099975623&partnerID=8YFLogxK
U2 - 10.1002/anie.202013039
DO - 10.1002/anie.202013039
M3 - Article
C2 - 33290612
AN - SCOPUS:85099975623
SN - 1433-7851
VL - 60
SP - 8859
EP - 8866
JO - Angewandte Chemie - International Edition
JF - Angewandte Chemie - International Edition
IS - 16
ER -