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. CD 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.