4.8 Article

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

Journal

JOURNAL OF THE AMERICAN CHEMICAL SOCIETY
Volume 143, Issue 17, Pages 6323-6327

Publisher

AMER CHEMICAL SOC
DOI: 10.1021/jacs.1c00342

Keywords

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Funding

  1. EPSRC Programme Grant (NOtCH) [EP/L027151/1]
  2. Leverhulme Trust
  3. Marie Curie FP7 ITN (SASSYPOL) [607602]

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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.
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.

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