The ability to use bio-inspired building-blocks in the assembly of novel supramolecular frameworks is at the forefront of this exciting research field. Herein, we present the first helical polyproline peptide to self-assemble to form a reversibly porous, crystalline, supramolecular peptide framework (SPF). This framework is assembled from a short oligoproline, adopting the polyproline II conformation, driven by hydrogen-bonding and pi-interactions. Thermal activation, guest-induced dynamic porosity and enantioselective guest inclusion have been demonstrated for this novel system. The principles of the self-assembly associated with this SPF will be used as a blueprint allowing for the further development of helical, proline-based peptide linkers in the rational design of SPFs and metal-peptide frameworks.
Herein, we present the first high resolution single crystal structure of an unfunctionalized tetrameric proline in the poly-proline II conformation. This rationally designed oligoproline tetramer, self-assembles to form a permanently porous crys-talline supramolecular peptide framework (SPF). Thermal activation, guest inclusion and thermally induced release of chemical guests have been demonstrated for this novel system. This discovery provides a conclusive insight into the pre-viously ambiguous conformation of short oligoprolines and will allow for the further development of proline-based pep-tide linkers in the rational design of SPFs and metal-peptide frameworks.
scite is a Brooklyn-based organization that helps researchers better discover and understand research articles through Smart Citations–citations that display the context of the citation and describe whether the article provides supporting or contrasting evidence. scite is used by students and researchers from around the world and is funded in part by the National Science Foundation and the National Institute on Drug Abuse of the National Institutes of Health.