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

David E. Clarke | Zendy; Guanglu Wu | Zendy; Ce Wu | Zendy; Oren A. Scherman | Zendy

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

Author(s) -

David E. Clarke,

Guanglu Wu,

Ce Wu,

Oren A. Scherman

Publication year - 2021

Publication title -

journal of the american chemical society

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 7.115

H-Index - 612

eISSN - 1520-5126

pISSN - 0002-7863

DOI - 10.1021/jacs.1c00342

Subject(s) - chemistry , peptide , sequence (biology) , folding (dsp implementation) , chirality (physics) , peptide sequence , oligopeptide , protein folding , amino acid , stereochemistry , combinatorial chemistry , biochemistry , physics , chiral symmetry breaking , quantum mechanics , quark , nambu–jona lasinio model , electrical engineering , gene , engineering

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.

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