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Updated: Jul 19, 2026

Production and Visualization of Bacterial Spheroplasts and Protoplasts to Characterize Antimicrobial Peptide Localization
Published on: August 11, 2018
Mechanism of supported membrane disruption by antimicrobial peptide protegrin-1
Kin Lok H Lam1, Yuji Ishitsuka, Yishan Cheng
1Department of Physics, The Institute for Biophysical Dynamics, and The James Franck Institute, The University of Chicago, Illinois 60637, USA.
Abstract:
While pore formation has been suggested as an important step in the membrane disruption process induced by antimicrobial peptides, membrane pore formation has never been directly visualized. We report on the dynamics of membrane disruption by antimicrobial peptide protegrin-1 (PG-1) on dimyristoyl-sn-glycero-phosphocholine-supported bilayer patches obtained via atomic force microscopy. The action of PG-1 is found to be concentration-dependent. At low PG-1 concentrations (1 < [PG-1] < 4 microg/mL), the peptide destabilizes the edge of the membrane to form fingerlike structures. At higher concentrations, PG-1 induces the formation of a sievelike nanoporous structure in the membrane. The highest degree of disruption is attained at concentrations >or=20 microg/mL, at which PG-1 disrupts the entire membrane, transforming it into stripelike structures with a well-defined and uniform stripe width. This first direct visualization of these membrane structural transformations helps elucidate the PG-1-induced membrane disruption mechanism.
Insights
Antimicrobial peptide protegrin-1 (PG-1) directly visualizes membrane disruption. PG-1 concentration dictates membrane changes, forming fingerlike, nanoporous, or stripelike structures, revealing its disruption mechanism.
Area of Science:
- Biophysics
- Membrane Biology
- Antimicrobial Peptides
Background:
- Antimicrobial peptides (AMPs) are crucial for innate immunity.
- Membrane disruption is a proposed mechanism for AMP action.
- Direct visualization of AMP-induced membrane pore formation has been lacking.
Purpose of the Study:
- To directly visualize the membrane disruption dynamics induced by the antimicrobial peptide protegrin-1 (PG-1).
- To elucidate the concentration-dependent mechanism of PG-1-induced membrane alteration.
Main Methods:
- Atomic force microscopy (AFM) was used to observe supported lipid bilayer patches.
- Dimyristoyl-sn-glycero-phosphocholine (DMPC) lipid bilayers were employed.
- Real-time imaging captured the structural transformations upon PG-1 addition.
Main Results:
- PG-1 induced concentration-dependent membrane structural changes.
- Low PG-1 concentrations (<4 microg/mL) led to edge destabilization and fingerlike structures.
- Higher PG-1 concentrations induced nanoporous or stripelike membrane structures, with complete disruption at >=20 microg/mL.
Conclusions:
- This study provides the first direct visualization of antimicrobial peptide-induced membrane disruption.
- The findings reveal a concentration-dependent mechanism for PG-1 action on lipid bilayers.
- Understanding these dynamics is key to developing new antimicrobial peptide-based therapies.
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