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pH-Dependent Packing Mode Variations and Chirality Inversion in Short Peptide Self-Assembly.

Xiaoyue Ma1, Kai Qi1, Xinfeng Ju1

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Summary

Researchers designed amphiphilic peptides that self-assemble into beta-sheet nanofibrils. Their helix handedness inverts with pH changes due to histidine protonation, offering control over chiral self-assembly.

Keywords:
Chirality inversionPacking modesShort amphiphilic peptidesSide‐chain interactionsβ‐sheet assembly

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Area of Science:

  • Biomaterials Science
  • Supramolecular Chemistry
  • Chemical Biology

Background:

  • Controlling peptide self-assembly structures and morphologies is a significant challenge.
  • Amphiphilic peptides offer tunable self-assembly properties.
  • Understanding chirality in self-assembled peptide systems is crucial for advanced materials.

Purpose of the Study:

  • To investigate the pH-dependent self-assembly and chirality inversion of designed amphiphilic peptides.
  • To elucidate the molecular mechanisms underlying pH-induced helix inversion in peptide nanofibrils.
  • To explore strategies for engineering hierarchical chirality in peptide assemblies.

Main Methods:

  • Design and synthesis of amphiphilic peptides (I3H).
  • Characterization using microscopy, neutron scattering, and spectroscopy.
  • Mechanistic studies involving pH titration, NMR, and molecular dynamics simulations.

Main Results:

  • Peptides self-assemble into beta-sheet nanofibrils with pH-dependent helix handedness inversion.
  • Histidine protonation state dictates antiparallel (low pH) vs. parallel (high pH) beta-sheet packing.
  • Pi-pi stacking of deprotonated histidine drives chiral flipping and supramolecular helix inversion.
  • Glycine insertion at the interface modulates the pH-dependent inversion effect.

Conclusions:

  • The study reveals a mechanism for pH-dependent chirality inversion in peptide self-assembly driven by histidine interactions.
  • Precise control over molecular packing and side-chain interactions enables the design of hierarchical chirality.
  • This work provides a blueprint for designing functional peptide-based nanomaterials with tunable chiral properties.