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Development of Antimicrobial Stapled Peptides Based on Magainin 2 Sequence.

Motoharu Hirano1,2, Chihiro Saito3, Hidetomo Yokoo1

  • 1Division of Organic Chemistry, National Institute of Health Sciences, 3-25-26, Tonomachi, Kawasaki, Kanagawa 210-9501, Japan.

Molecules (Basel, Switzerland)
|January 20, 2021
PubMed
Summary

Hydrocarbon stapling stabilized antimicrobial peptides derived from Magainin 2 (Mag2), enhancing their helical structure and antimicrobial activity. Stapled peptide 2 demonstrated superior efficacy against bacteria with low hemolytic activity.

Keywords:
amphipathicityantimicrobial peptideshelical structuremagainin 2stapled peptide

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Area of Science:

  • Biochemistry
  • Peptide Chemistry
  • Microbiology

Background:

  • Magainin 2 (Mag2), an antimicrobial peptide (AMP), disrupts microbial membranes.
  • Helicity and amphipathicity are crucial for Mag2's antimicrobial function.
  • Previous work identified 17 amino acid residues essential for Mag2 activity and developed related foldamers.

Purpose of the Study:

  • To design and synthesize Mag2 derivatives with hydrocarbon stapling for enhanced helix stabilization.
  • To evaluate the secondary structures, antimicrobial, and cell-membrane disruption activities of these novel peptides.
  • To investigate the mechanism of action for stapled peptides regarding their antimicrobial and hemolytic effects.

Main Methods:

  • Synthesis of Mag2 derivatives with hydrocarbon stapling side chains.
  • Evaluation of secondary structures using biophysical techniques.
  • Antimicrobial assays against gram-positive and gram-negative bacteria.
  • Cell-membrane disruption assays and hemolytic activity tests.
  • Electrophysiological measurements to probe mechanisms of action.

Main Results:

  • Hydrocarbon stapling significantly stabilized the helical structure of Mag2 derivatives.
  • Stapling enhanced the overall antimicrobial activity of the designed peptides.
  • Peptide 2, stapled between the first and fifth positions, exhibited enhanced antimicrobial activity against both gram-positive and gram-negative bacteria.
  • Peptide 2 displayed minimal hemolytic activity compared to the native Mag2.
  • Electrophysiological studies provided insights into the membrane interaction mechanisms.

Conclusions:

  • Hydrocarbon stapling is an effective strategy to stabilize helical antimicrobial peptides and boost their efficacy.
  • Stapled Mag2 derivatives, particularly peptide 2, represent promising candidates for novel antimicrobial agents with improved safety profiles.
  • Further investigation into the structure-activity relationships and mechanisms of action of these stapled peptides is warranted.