Metalloprotein-inspired design of synthetic polymers.

Abstract

Metal ion recognition in proteins emerges from coordinated effects of sequence patterning, hierarchical structure, and dynamic plasticity that promote high-affinity, ion-selective binding. Synthetic polymers, by contrast, offer broad chemical tunability but lack unified frameworks linking copolymer sequence and organization to function. Here, we position lanthanide-binding polymers as a tractable, technologically relevant model for importing protein-inspired design principles into synthetic macromolecules. We summarize approaches to quantify monomer patterning beyond coarse architectural classifications, enabling direct connections between polymer sequence and function. Using metalloproteins as conceptual inspiration, we examine coordination-dependent hierarchical structures in synthetic polymers, where noncovalent interactions drive reorganization across local and global length scales. We then highlight chain dynamics as an underexplored dimension of macromolecular design, where ion-dependent changes in mobility may couple to affinity and selectivity. Together, these sequence-structure-dynamics relationships provide a framework for developing polymeric chelators with protein-like metal recognition for applications in sensing, separations, and catalysis.