Host–Guest Induced Peptide Folding with Sequence-Specific Structural Chirality

Image credit: ACS


Controlling the spatial and temporal behavior of peptide segments is essential in the fabrication of functional peptide-based materials and nanostructures. To achieve a desired structure, complex sequence design is often required, coupled with the inclusion of unnatural amino acids or synthetic modifications. Herein, we investigate the structural properties of 1:1 inclusion complexes between specific oligopeptides and cucurbit[8]uril (CB[8]), inducing the formation of turns, and by alteration of the peptide sequence, tunable structural chirality. We also explore extended peptide sequence binding with CB[8], demonstrating a simple approach to construct a peptide hairpin.

Guanglu Wu
Guanglu Wu
Principal Investigator

Research interests: multi-component functional assemblies, noncovalent dimerization, supramolecular catalysis, and smart soft matter