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A Bioinspired Mastoparan Exhibits Concentration-Dependent Anti-Bacterial Activity via Membrane Disruption

Rodrigues, Gisele R. ; Fornasier, Marco LU orcid ; Caselli, Lucrezia LU ; Malmsten, Martin LU ; Sparr, Emma LU ; Jönsson, Peter LU and Franco, Octavio L. LU (2025) In ACS Applied Materials and Interfaces 17(49). p.66235-66248
Abstract

Antimicrobial peptides are widely investigated in the literature, but their mechanism of action and effects on lipid membranes are not completely understood from a physicochemical perspective. In this study, we employed a bioinspired mastoparan from wasp venom, mast-MO, and characterized its interactions with model lipid membranes, either as a supported lipid bilayer or as free-standing vesicles in solution. An array of complementary physicochemical characterization techniques was employed to study the surface activity of the peptide alone and how its adsorption affects lipid membrane properties in terms of lateral organization and integrity. We found that peptide action is related to its intrinsic surface activity, resulting in... (More)

Antimicrobial peptides are widely investigated in the literature, but their mechanism of action and effects on lipid membranes are not completely understood from a physicochemical perspective. In this study, we employed a bioinspired mastoparan from wasp venom, mast-MO, and characterized its interactions with model lipid membranes, either as a supported lipid bilayer or as free-standing vesicles in solution. An array of complementary physicochemical characterization techniques was employed to study the surface activity of the peptide alone and how its adsorption affects lipid membrane properties in terms of lateral organization and integrity. We found that peptide action is related to its intrinsic surface activity, resulting in disrupted lipid packing of supported membranes and vesicles via a concentration-dependent mechanism. Changing solution conditions, e.g., ionic strength and pH, altered the electrostatic interactions between the membrane and mast-MO, resulting in less significant adsorption. This mechanism of action was also validated in vitro for Gram-negative E. coli bacteria, demonstrating rapid action (within 15 min) and potent antimicrobial activity. These results provide new information on the molecular effects of mastoparan’s interactions with membranes.

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author
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organization
publishing date
type
Contribution to journal
publication status
published
subject
keywords
antimicrobial peptides, bacteria, lipid membranes, mastoparans, membranolytic effect
in
ACS Applied Materials and Interfaces
volume
17
issue
49
pages
14 pages
publisher
The American Chemical Society (ACS)
external identifiers
  • scopus:105024469885
  • pmid:41283220
ISSN
1944-8244
DOI
10.1021/acsami.5c14290
language
English
LU publication?
yes
additional info
Publisher Copyright: © 2025 The Authors. Published by American Chemical Society
id
8b213cce-8f08-400b-aee4-8bd5bb3b54d9
date added to LUP
2026-02-11 16:27:35
date last changed
2026-02-11 16:28:30
@article{8b213cce-8f08-400b-aee4-8bd5bb3b54d9,
  abstract     = {{<p>Antimicrobial peptides are widely investigated in the literature, but their mechanism of action and effects on lipid membranes are not completely understood from a physicochemical perspective. In this study, we employed a bioinspired mastoparan from wasp venom, mast-MO, and characterized its interactions with model lipid membranes, either as a supported lipid bilayer or as free-standing vesicles in solution. An array of complementary physicochemical characterization techniques was employed to study the surface activity of the peptide alone and how its adsorption affects lipid membrane properties in terms of lateral organization and integrity. We found that peptide action is related to its intrinsic surface activity, resulting in disrupted lipid packing of supported membranes and vesicles via a concentration-dependent mechanism. Changing solution conditions, e.g., ionic strength and pH, altered the electrostatic interactions between the membrane and mast-MO, resulting in less significant adsorption. This mechanism of action was also validated in vitro for Gram-negative E. coli bacteria, demonstrating rapid action (within 15 min) and potent antimicrobial activity. These results provide new information on the molecular effects of mastoparan’s interactions with membranes.</p>}},
  author       = {{Rodrigues, Gisele R. and Fornasier, Marco and Caselli, Lucrezia and Malmsten, Martin and Sparr, Emma and Jönsson, Peter and Franco, Octavio L.}},
  issn         = {{1944-8244}},
  keywords     = {{antimicrobial peptides; bacteria; lipid membranes; mastoparans; membranolytic effect}},
  language     = {{eng}},
  month        = {{12}},
  number       = {{49}},
  pages        = {{66235--66248}},
  publisher    = {{The American Chemical Society (ACS)}},
  series       = {{ACS Applied Materials and Interfaces}},
  title        = {{A Bioinspired Mastoparan Exhibits Concentration-Dependent Anti-Bacterial Activity via Membrane Disruption}},
  url          = {{http://dx.doi.org/10.1021/acsami.5c14290}},
  doi          = {{10.1021/acsami.5c14290}},
  volume       = {{17}},
  year         = {{2025}},
}