Self-assembled peptides provide a powerful blueprint for the design of complex synthetic materials. Previously, peptide–metal frameworks using short sequences (≤ 3 residues) have shown great promise as proteomimetic materials that exhibit sophisticated capabilities. However, their evolution has been hindered due to few mutable residues and restricted choice of side-chains that are compatible with metal ions. Herein, we developed a non-covalent strategy using π-stacking to assemble longer peptides into crystalline frameworks that tolerate several mutations with diverse functionalities. These materials exhibit hallmark protein behaviors such as guest-selective induced-fit and assembly of multi-metallic units. Significantly, we demonstrate facile evolution of the framework to substantially increase affinity towards a complex organic molecule.

Assembly of π-conjugated peptides into a porous and evolvable protein-like lattice

Fall 2022 abstracts, posters, and presentations will launch in mid-September.

ACS Fall 2022

The official archive and repository for all ACS Meetings & Expositions abstracts and select posters or presentations.