Host–Guest Induced Peptide Folding with Sequence-Specific Structural Chirality
David E. Clarke, Guanglu Wu, Ce Wu, Oren A. Scherman
Abstract
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.
Topics & Concepts
ChemistryPeptideSequence (biology)Folding (DSP implementation)Chirality (physics)Peptide sequenceOligopeptideProtein foldingAmino acidStereochemistryCombinatorial chemistryBiochemistryPhysicsNambu–Jona-Lasinio modelQuarkQuantum mechanicsGeneEngineeringElectrical engineeringChiral symmetry breakingSupramolecular Self-Assembly in MaterialsSupramolecular Chemistry and ComplexesChemical Synthesis and Analysis