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Related Experiment Video

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Construction of Cyclic Cell-Penetrating Peptides for Enhanced Penetration of Biological Barriers
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Membrane targeting antimicrobial cyclic peptide nanotubes - an experimental and computational study.

Bárbara Claro1, Eva González-Freire2, Martin Calvelo2

  • 1CIQUP, Centro de Investigação em Química, Departamento de Química e Bioquímica, Faculdade de Ciências, Universidade do Porto, Porto, Portugal.

Colloids and Surfaces. B, Biointerfaces
|September 29, 2020
PubMed
Summary

Cyclic peptides (CPs) interact strongly with negatively charged membranes, forming nanotubes. This discovery aids in developing new antimicrobial peptides to combat resistant pathogens.

Keywords:
ATR-FTIRAntimicrobial peptidesCoarse-GrainedD,L-α-cyclic peptidesDSCMolecular dynamic simulationsNanotubesSelf-Assembly

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Area of Science:

  • Biochemistry
  • Materials Science
  • Pharmacology

Background:

  • Antibiotic resistance is a major public health threat, necessitating novel antimicrobial agents.
  • Antimicrobial peptides (AMPs) offer a new paradigm, targeting microbial membranes.
  • Cyclic peptides (CPs) show promise due to protease resistance and self-assembly into nanotubes (SCPNs).

Purpose of the Study:

  • To investigate the interaction mechanism of cyclic peptides (CPs) with model lipid membranes.
  • To characterize the self-assembly of CPs into Self-assembled Cyclic Peptide Nanotubes (SCPNs) on membranes.
  • To understand the influence of membrane charge on CP-membrane interactions and SCPN formation.

Main Methods:

  • Differential Scanning Calorimetry (DSC) to assess membrane-peptide interactions.
  • Attenuated Total Reflectance Fourier-Transform Infrared Spectroscopy (ATR-FTIR) for structural analysis.
  • Coarse-grained molecular dynamics (CG-MD) simulations to model interactions and nanotube formation.

Main Results:

  • CPs exhibit strong interactions with negatively charged membranes, with interaction strength dependent on peptide and membrane charge.
  • CPs primarily adopt a β-structure upon self-assembly at the membrane surface.
  • CG-MD simulations confirmed experimental findings on nanotube formation, orientation, and membrane charge dependence.

Conclusions:

  • CPs effectively interact with and self-assemble on negatively charged membranes, forming nanotubes.
  • Membrane electrostatic charge significantly influences CP interaction and SCPN formation.
  • These findings provide a basis for designing next-generation cyclic peptides with enhanced antimicrobial activity and reduced toxicity.