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Molecular mechanisms of membrane perturbation by antimicrobial peptides and the use of biophysical studies in the design of novel peptide antibiotics.
Abstract
Antibiotic resistant bacterial strains represent a global health problem with a strong social and economic impact. Thus, there is an urgent need for the development of antibiotics with novel mechanisms of action. There is currently an extensive effort to understand the mode of action of antimicrobial peptides which are considered as one alternative to classical antibiotics. The main advantage of this class of substances, when considering bacterial resistance, is that they rapidly, within minutes, kill bacteria. Antimicrobial peptides can be found in every organism and display a wide spectrum of activity. Hence, the goal is to engineer peptides with an improved therapeutic index, i.e. high efficacy and target specificity. For the rational design of such novel antibiotics it is essential to elucidate the molecular mechanism of action. Biophysical studies have been performed using to a large extent membrane model systems demonstrating that there are distinctive different mechanisms of bacterial killing by antimicrobial peptides. One can distinguish between peptides that permeabilize and/or disrupt the bacterial cell membrane and peptides that translocate through the cell membrane and interact with a cytosolic target. Lantibiotics exhibit specific mechanisms, e.g. binding to lipid II, a precursor of the peptidoglycan layer, either resulting in membrane rupture by pore formation or preventing cell wall biosynthesis. The classical models of membrane perturbation, pore formation and carpet mechanism, are discussed and related to other mechanisms that may lead to membrane dysfunction such as formation of lipid-peptide domains or membrane disruption by formation of non-lamellar phases. Emphasis is on the role of membrane lipid composition in these processes and in the translocation of antimicrobial peptides.
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“Most of them act as proton gradient perturbing molecules, (causing membrane depolarization like polymyxin B and colistin; Lohner and Blondelle, 2005)”
From Bioactive Molecules Released in Food by Lactic Acid Bacteria: Encrypted Peptides and Biogenic Amines (2016) · cites this paper as Lohner and Blondelle, 2005
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Metadata
- Authors
- Lohner, K., & Blondelle, S.
- Affiliations
- Austrian Academy of Sciences (AT)
- Venue
- Combinatorial Chemistry & High Throughput Screening
- Publisher
- Bentham Science Publishers Ltd.
- Published
- 2005-05-01
- Volume
- 8
- Issue
- 3
- Pages
- 241-256
- ISSN
- 1386-2073 (ISSN-L)
- OpenAlex
- W2045743453
- Cited by
- 222
- References
- 0
- Citations by year
- 2026: 4 · 2025: 4 · 2024: 7 · 2023: 2 · 2022: 4 · 2021: 8 · 2020: 9 · 2019: 14 · 2018: 4 · 2017: 9 · 2016: 10 · 2015: 5 · 2014: 12 · 2013: 11 · 2012: 13
- FWCI
- 17.28
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Combinatorial Chemistry & High Throughput Screening (publishedVersion)
- PubMed (publishedVersion)
- Topics
- Life Sciences › Immunology and Microbiology › Microbiology › Antimicrobial Peptides and Activities
- Life Sciences › Immunology and Microbiology › Applied Microbiology and Biotechnology › Antimicrobial agents and applications
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › RNA Interference and Gene Delivery
- Keywords
- antimicrobial peptides, membrane perturbation, antibiotic resistance, peptide antibiotics, lantibiotics, pore formation, carpet mechanism, membrane permeabilization, lipid II, membrane lipid composition, peptide translocation, model membranes, peptide engineering, bacterial membranes
- MeSH terms
- Anti-Infective Agents, Anti-Bacterial Agents, Cell Membrane, Membrane Lipids, Peptidoglycan, Structure-Activity Relationship, Drug Design, Combinatorial Chemistry Techniques, Antimicrobial Cationic Peptides
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