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

Controlling the spatial and temporal behavior of peptide segments is essential in the fabrication of functional peptidebased 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.

Automated summary

Control of spatial and temporal behavior of peptide segments is crucial in fabricating functional peptide-based materials and nanostructures. Complex sequence design and inclusion of unnatural amino acids or synthetic modifications are often required to achieve desired structures. In this study, the structural properties of 1:1 inclusion complexes between specific oligopeptides and CB[8] were investigated, showing induction of turns and tunable structural chirality by altering peptide sequences. Extension of peptide sequence binding with CB[8] was also explored as a simple method to construct a peptide hairpin.