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Related Experiment Video

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Membrane-Disrupting Nanofibrous Peptide Hydrogels.

Biplab Sarkar1, Zain Siddiqui1, Peter K Nguyen1

  • 1Department of Biomedical Engineering, New Jersey Institute of Technology, Newark, New Jersey 07102-1982, United States.

ACS Biomaterials Science & Engineering
|January 15, 2021
PubMed
Summary

Cationic amphiphilic self-assembled peptides (CASPs) form hydrogels that disrupt bacterial membranes. These self-assembled peptide nanofibers offer tunable material properties for potential antimicrobial applications.

Keywords:
antimicrobial peptideshydrogelmembrane disruptionnoncovalent cross-linkingpeptide nanofibersself-assembly

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Area of Science:

  • Biomaterials Science
  • Supramolecular Chemistry
  • Antimicrobial Engineering

Background:

  • Natural antimicrobial peptides inspire new biomaterials.
  • Self-assembled peptide nanofibers form hydrogels via noncovalent interactions.
  • Cationic amphiphilic self-assembled peptides (CASPs) are designed for bacterial membrane disruption.

Purpose of the Study:

  • Investigate self-assembly of CASP nanofibers into hydrogels.
  • Characterize material properties of nanofibers and bulk hydrogels.
  • Evaluate the antimicrobial efficacy and mechanism against bacteria.

Main Methods:

  • Atomic force microscopy for nanomechanical analysis.
  • Rheometry for bulk hydrogel viscoelastic properties.
  • Coarse-grained simulations for peptide-membrane interactions.

Main Results:

  • CASP nanofibers form viscoelastic hydrogels with tunable properties.
  • Hydrogel properties depend on peptide concentration, ionic strength, and cross-linker concentration.
  • CASP nanofibers disrupt bacterial membranes by stiffening, contraction, and osmotic imbalance.

Conclusions:

  • Self-assembled peptide nanofibers offer tunable material properties.
  • CASP hydrogels demonstrate antimicrobial efficacy through membrane disruption.
  • These injectable hydrogels show potential as novel antimicrobial agents.