Cited by 222Antimicrobial Peptides and ActivitiesAntimicrobial agents and applicationsRNA Interference and Gene Delivery

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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.

Lohner, K., Blondelle, S.·2005·Combinatorial Chemistry & High Throughput Screening

DOI 10.2174/1386207053764576

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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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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)
DOI: 10.2174/1386207053764576
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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Molecular mechanisms of membrane perturbation by antimicrobial peptides and the use of biophysical studies in the design of novel peptide antibiotics.

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