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Related Experiment Video

Updated: May 7, 2026

Formation of Ordered Biomolecular Structures by the Self-assembly of Short Peptides
07:26

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Published on: November 21, 2013

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Charge regulation in peptide self-assembly and hydrogelation.

Luigi Gentile1, Birgitta Frohm2, Anders Malmendal3

  • 1Department of Chemistry, University of Bari Aldo Moro, Via Orabona 4, 70126 Bari, Italy; Center of Colloid and Surface Science (CSGI), Bari Unit, Via Orabona 4, 70126 Bari, Italy.

Journal of Colloid and Interface Science
|August 7, 2025
PubMed
Summary

The peptide Ac-KGSFSIQYTYHVD-CONH₂ (KD) forms pH-responsive hydrogels by self-assembling into beta-sheet fibrils. Its mechanical properties are tunable with pH, showing potential for biomaterial applications.

Keywords:
HydrogelationPeptideSelf-assemblyStimuli-responsivepH-responsive

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Area of Science:

  • Biomaterials Science
  • Supramolecular Chemistry
  • Biophysics

Background:

  • Peptide self-assembly is a key mechanism for creating advanced biomaterials.
  • Understanding the pH-dependent structural transitions of peptides is crucial for controlling hydrogel properties.
  • Human semenogelin I-derived peptides offer potential for novel hydrogel development.

Purpose of the Study:

  • To investigate the pH-dependent self-assembly mechanism of the peptide Ac-KGSFSIQYTYHVD-CONH₂ (KD).
  • To elucidate the structural evolution and mechanical property modulation of KD-based hydrogels.
  • To explore the potential of KD hydrogels for therapeutic applications.

Main Methods:

  • Time-resolved nuclear magnetic resonance (NMR) spectroscopy to monitor structural changes.
  • Cryo-transmission electron microscopy (cryo-TEM) for visualizing nanostructures.
  • Rheological studies to quantify mechanical properties under varying pH.
  • pH measurements to track peptide interactions during gelation.

Main Results:

  • KD self-assembles into beta-sheet fibrils, forming a hydrogel network.
  • Two distinct nanostructures (fibrils and curly nanostructures) were observed via cryo-TEM.
  • A significant increase in elastic modulus was correlated with pH shifts.
  • The peptide exhibited rapid hydrogel formation under buffered conditions.

Conclusions:

  • The pH-responsive hydrogel formation of KD is primarily driven by histidine protonation.
  • KD hydrogels demonstrate dynamic tunability of mechanical properties.
  • These findings provide mechanistic insights for designing peptide-based biomaterials for therapeutic use.