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Related Experiment Video

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Nanoscale Assembly of Functional Peptides with Divergent Programming Elements.

Ana M Garcia1, Michele Melchionna1,2, Ottavia Bellotto1

  • 1Chemical and Pharmaceutical Sciences Department, University of Trieste, Via Giorgieri 1, 34127 Trieste, Italy.

ACS Nano
|February 12, 2021
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Summary

Chirality in self-assembling peptides directs nanostructure formation and influences amyloid aggregation. This study explores eight Pro-Phe-Phe stereoisomers for biomedical and nanotechnology applications.

Keywords:
amyloidchiralityd-amino acidshydrogelspeptideprolineself-assembly

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Area of Science:

  • Biomaterials Science
  • Nanotechnology
  • Molecular Biology

Background:

  • Self-assembling peptides are crucial in biomedicine and nanotechnology, with their function dictated by self-assembly modes.
  • Contrasting structural elements, proline (a β-breaker) and diphenylalanine (a β-structure motif), were combined in a tripeptide sequence.

Purpose of the Study:

  • To investigate how amino acid chirality influences the self-assembly of a novel tripeptide containing proline and diphenylalanine.
  • To explore the potential of these self-assembling peptides in forming diverse nanostructures and their interaction with amyloid aggregation.

Main Methods:

  • Synthesis and characterization of eight Pro-Phe-Phe stereoisomers.
  • Analysis of self-assembly into nanoparticles, nanotapes, and fibrils using single-crystal structures and molecular dynamics simulations.
  • In vitro testing of stereoisomers for inhibition of Alzheimer's disease-associated amyloid-beta (Aβ(1-42)) peptide fibrillization.

Main Results:

  • Stereoconfiguration of Pro-Phe-Phe peptides dictated the formation of distinct nanostructures (nanoparticles, nanotapes, fibrils) and hydrogel properties.
  • Molecular simulations elucidated the interactions driving assembly at different ranges (short, medium, long).
  • One specific stereoisomer effectively inhibited Aβ(1-42) fibrillization via multivalent diphenylalanine binding.

Conclusions:

  • Heterochirality is a key design feature for controlling peptide self-assembly and nanostructure formation.
  • These findings suggest potential therapeutic applications for modulating pathological amyloid aggregation.
  • The developed peptides exhibit protease resistance and biocompatibility, enhancing their therapeutic potential.