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Updated: Jul 16, 2026

Synthesis and Characterization of 1,2-Dithiolane Modified Self-Assembling Peptides
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Enhancing the Antimicrobial Potency of Self-Assembling Antibiotics by Co-Assembly-Based Aggregation Modulation.

Bodhisattwa Das Gupta1, Rahul Kuiri1, Thangavel Vijayakanth2,3

  • 1Department of Biotechnology, National Institute of Technology Durgapur, A-Zone, Mahatma Gandhi Road, Durgapur, West Bengal, India.

Macromolecular Bioscience
|July 15, 2026
PubMed
Summary

Modulating antimicrobial peptide (AMP) interactions enhances their potency. Co-assembling Fmoc-phenylalanine with Fmoc-glutamic acid broadens its antibacterial spectrum by disrupting bacterial membranes.

Keywords:
MD simulationantimicrobial peptideshydrogelspeptide adjuvantspeptides co‐assembly

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Published on: February 6, 2020

Area of Science:

  • Biochemistry
  • Materials Science
  • Microbiology

Background:

  • Antimicrobial peptides (AMPs) show promise as alternatives to conventional antibiotics.
  • AMP activity is influenced by aggregation; weaker associations enhance function, while stable assemblies decrease it.
  • Modulating intermolecular interactions is a potential strategy to boost AMP efficacy.

Purpose of the Study:

  • To develop a general strategy for enhancing AMP potency.
  • To broaden the activity spectrum of a Gram-positive-specific AMP, Fmoc-phenylalanine.
  • To investigate the role of co-assembly with non-antibiotic peptides in modulating AMP function.

Main Methods:

  • Co-assembly of Fmoc-phenylalanine with Fmoc-glutamic acid.
  • Biophysical assays to assess membrane disruption and cell death.
  • Rheological measurements to evaluate hydrogel mechanical rigidity.
  • Molecular dynamics simulations to analyze fibril stability and interactions.

Main Results:

  • Co-assembly broadened the activity spectrum of Fmoc-phenylalanine against Gram-positive bacteria.
  • The co-assembled system effectively disrupted bacterial membrane integrity, causing cell death.
  • Enhanced potency correlated with reduced hydrogel mechanical rigidity.
  • Molecular dynamics simulations indicated that heterogeneous non-covalent interactions destabilized peptide fibrils.

Conclusions:

  • Rationally designed co-assembling partners can weaken stabilizing non-covalent interactions.
  • This weakening effect enhances the antibacterial efficacy of existing AMPs.
  • Co-assembly presents a common strategy to improve AMP potency and broaden their spectrum of activity.