Designing Enzyme-Like Catalysts: A Rhodium(II) Metallopeptide Case Study

Stereoselective Self-Assembly of DNA Binding Helicates Directed by the Viral β-Annulus Trimeric Peptide Motif

“…Peptides are ideal platforms for the programmed assembly of supramolecular structures, as they encode in their sequences precise structural and functional information in their sequence. Several peptide motifs, such as coiled-coils, β-hairpins, or amphiphilic peptides, have been studied as the basis for biofunctional devices and materials. − However, despite the enormous potential for the control of stereochemistry, nuclearity, and stoichiometry, the assembly of metal complexes driven by peptide motifs has only started to take off, − and most examples in the literature are restricted to systems based on coiled-coils. − As a test case to show the potential of peptide motifs to direct the assembly of metal complexes, we focused our attention on helicates, which are discrete metal complexes in which one or more organic ligands coordinate two or more metal ions, − because of their interest in supramolecular chemistry and exciting biological applications. − Helicates are inherently chiral species that can show right-handed (designated as P ) or left-handed ( M ) helicity, according to the orientation in which the ligands coil around the axis defined by the metal centers. Indeed, one of the biggest challenges for the synthesis of helicates is their stereoselective assembly with controlled supramolecular chirality. − In this context, we wanted to test whether a small trimeric peptide motif could effectively control the self-assembly of three-stranded peptide helicates, selecting a particular orientation of the ligand chains and helical chirality.…”