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 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 modi...

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Bibliographic Details
Published inJournal of the American Chemical Society Vol. 143; no. 17; pp. 6323 - 6327
Main Authors Clarke, David E, Wu, Guanglu, Wu, Ce, Scherman, Oren A
Format Journal Article
LanguageEnglish
Published United States American Chemical Society 05.05.2021
Subjects
Amino Acid Sequence
Bridged-Ring Compounds - chemistry
Circular Dichroism
Communication
Fluorescence Resonance Energy Transfer
Models, Molecular
Peptides - chemistry
Protein Folding
Stereoisomerism
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Summary: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.
Bibliography:ObjectType-Article-1
SourceType-Scholarly Journals-1
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ISSN:0002-7863
1520-5126
1520-5126
DOI:10.1021/jacs.1c00342