Hydrogen-Bonding-Driven 3D Supramolecular Assembly of Peptidomimetic Zipper

Hydrogen-bonding-driven
three-dimensional (3D) assembly of a peptidomimetic
zipper has been established for the first time by using an α/AApeptide
zipper that assembles into a de novo lattice arrangement
through two layers of hydrogen-bonded linker-directed interactions.
Via a covalently bridged 1D 413-helix, drastic enhancement
in stability has been achieved in the formed 3D crystalline supramolecular
architecture as evidenced by gas-sorption studies. As the first example
of an unnatural peptidic zipper, the dimensional augmentation of the
zipper differs from metal-coordinated strategies, and may have general
implications for the preparation of peptidic functional materials
for a variety of future applications.