Switching the Chirality of the Metal Environment Alters the Coordination Mode in Designed Peptides

摘要

De novo metallopeptide design contributes significantly to the understanding of protein folding, protein-protein interactions, and metal-ion sites in biology. Within this rubric, studies in our research group have been focused on the biochemistry of Cd~(II) thiolate sites. A class of peptides based on the parent peptide TRI, Ac-G(LKALEEK)4G-NH2, was designed to assemble in aqueous solution into amphophilic α-helices. These peptides aggregate to form three-stranded coiled coils above pH 5.5. Substitutions can be made to the interior of these coiled coils to generate metal-binding sites, potentially with adjacent cavities.