scholarly journals Mode-of-Action of Antimicrobial Peptides: Membrane Disruption vs. Intracellular Mechanisms

2020 ◽  
Vol 2 ◽  
Author(s):  
Aurélie H. Benfield ◽  
Sónia Troeira Henriques
Keyword(s):  
Antimicrobial Peptides ◽  
Physicochemical Properties ◽  
Broad Spectrum ◽  
Mode Of Action ◽  
Bacterial Pathogens ◽  
Model Membranes ◽  
Membrane Disruption ◽  
Attractive Alternative ◽  
Bacterial Cells

Antimicrobial peptides are an attractive alternative to traditional antibiotics, due to their physicochemical properties, activity toward a broad spectrum of bacteria, and mode-of-actions distinct from those used by current antibiotics. In general, antimicrobial peptides kill bacteria by either disrupting their membrane, or by entering inside bacterial cells to interact with intracellular components. Characterization of their mode-of-action is essential to improve their activity, avoid resistance in bacterial pathogens, and accelerate their use as therapeutics. Here we review experimental biophysical tools that can be employed with model membranes and bacterial cells to characterize the mode-of-action of antimicrobial peptides.

Revealing the Mode of Action of Halictine Antimicrobial Peptides: A Comprehensive Study with Model Membranes

Langmuir ◽  
2020 ◽  
Vol 36 (19) ◽  
pp. 5145-5155 ◽  
Author(s):  
Tatiana M. Domingues ◽  
Katia R. Perez ◽  
Karin A. Riske
Keyword(s):  
Antimicrobial Peptides ◽  
Mode Of Action ◽  
Model Membranes ◽  
Comprehensive Study

scholarly journals Mode of Action of the Antimicrobial Peptide Aureocin A53 from Staphylococcus aureus

2002 ◽  
Vol 68 (11) ◽  
pp. 5274-5280 ◽  
Author(s):  
Daili Jacqueline Aguilar Netz ◽  
Maria do Carmo de Freire Bastos ◽  
Hans-Georg Sahl
Keyword(s):  
Mode Of Action ◽  
Neutral Lipids ◽  
Membrane Damage ◽  
Model Membranes ◽  
Bacterial Cells ◽  
Gram Staining ◽  
Rapid Release ◽  
High Concentrations ◽  
Staphylococcus Simulans ◽  
Tryptophan Emission

ABSTRACT We investigated the mode of action of aureocin A53 on living bacterial cells and model membranes. Aureocin A53 acted bactericidally against Staphylococcus simulans 22, with >90% of the cells killed within a few minutes. Cell death was followed by lysis, as indicated by a clearing of the cell suspension and Gram staining. Aureocin A53 rapidly dissipated the membrane potential and simultaneously stopped biosynthesis of DNA, polysaccharides, and protein. Aureocin A53 induced a rapid release of preaccumulated glutamate and Rb+. Experiments on model membranes demonstrated that aureocin A53 provoked significant leakage of carboxyfluorescein (CF) exclusively from acidic liposomes but only at relatively high concentrations (0.5 to 8 mol%). Thus, the bactericidal activity of aureocin A53 derives from membrane permeation via generalized membrane destruction rather than by formation of discrete pores within membranes. Tryptophan emission fluorescence spectroscopy demonstrated interaction of aureocin A53 with both acidic and neutral membranes, as indicated by similar blue shifts. Since there was no significant aureocin A53-induced CF leakage from neutral liposomes, its appears that the peptide does interact with neutral lipids without provoking membrane damage.

scholarly journals Nanomechanical Characterization of the Synergism of Antimicrobial Peptides PGLa and Mag2 for Lipid Membrane Disruption

2021 ◽  
Vol 120 (3) ◽  
pp. 191a
Author(s):  
Fabio Perissinotto ◽  
Sebastien Janel ◽  
Javier Lopez-Alonso ◽  
Vincent Dupres ◽  
Burkhard Bechinger ◽  
...  
Keyword(s):  
Antimicrobial Peptides ◽  
Lipid Membrane ◽  
Membrane Disruption

scholarly journals Phage-encoded cationic antimicrobial peptide used for outer membrane disruption in lysis

2019 ◽  
Author(s):  
Ashley Holt ◽  
Jesse Cahill ◽  
Jolene Ramsey ◽  
Chandler O’Leary ◽  
Russell Moreland ◽  
...  
Keyword(s):  
Antimicrobial Peptides ◽  
Antimicrobial Peptide ◽  
Outer Membrane ◽  
Genetic Selection ◽  
Helical Structure ◽  
Bioinformatic Analysis ◽  
Membrane Disruption ◽  
Bacterial Cells ◽  
New Paradigm ◽  
Cationic Antimicrobial Peptide

AbstractSpanins are required for the last step in bacteriophage lysis: the disruption of the outer membrane. Bioinformatic analysis has shown that ~15% of phages lack a spanin gene, which suggests an alternate mechanism of outer membrane disruption. To address this, we selected virulent podophage ϕKT as a spaninless exemplar and tested ϕKT genes for outer membrane disruption during lysis. Hypothetical novel gene 28 causes outer membrane disruption when co-expressed with ϕKT lysis genes and complements the lysis defect of a λ spanin mutant. Gp28 is a 56 aa cationic peptide with predicted amphipathic helical structure and is associated with the particulate fraction after lysis. Urea and KCl washes did not release gp28 from the particulate, suggesting a strong hydrophobic interaction with the membrane. Super high-resolution microscopy supports a primarily outer membrane localization for the peptide. Additionally, holin function is not required for gp28-mediated lysis. Gp28 is similar in size, charge, predicted fold, and membrane association to the human cathelicidin antimicrobial peptide LL-37. In standard assays to measure bactericidal and inhibitory effects of antimicrobial peptides on bacterial cells, synthesized gp28 performed equivalently to LL-37. The studies presented here suggest that ϕKT Gp28 disrupts bacterial outer membranes during lysis in a manner akin to antimicrobial peptides.SignificanceHere we provide evidence that ϕKT produces an antimicrobial peptide for outer membrane disruption during lysis. The disruptin is a new paradigm for phage lysis, and has no similarities to other known lysis genes. Many mechanisms have been proposed for the function of antimicrobial peptides, however there is not a consensus on the molecular basis of membrane disruption. Additionally, there is no established genetic selection system to support such studies. Therefore, the ϕKT disruptin may represent the first genetically tractable antimicrobial peptide.

scholarly journals Biophysical characterization of the insertion of two potent antimicrobial peptides-Pin2 and its variant Pin2[GVG] in biological model membranes

2020 ◽  
Vol 1862 (2) ◽  
pp. 183105 ◽  
Author(s):  
Brandt Bertrand ◽  
Sathishkumar Munusamy ◽  
José-Francisco Espinosa-Romero ◽  
Gerardo Corzo ◽  
Iván Arenas Sosa ◽  
...  
Keyword(s):  
Antimicrobial Peptides ◽  
Model Membranes ◽  
Biological Model ◽  
Biophysical Characterization

scholarly journals Characterization of dual effects induced by antimicrobial peptides: Regulated cell death or membrane disruption

2012 ◽  
Vol 1820 (7) ◽  
pp. 1062-1072 ◽  
Author(s):  
Edgar J. Paredes-Gamero ◽  
Marta N.C. Martins ◽  
Fábio A.M. Cappabianco ◽  
Jaime S. Ide ◽  
Antonio Miranda
Keyword(s):  
Cell Death ◽  
Antimicrobial Peptides ◽  
Membrane Disruption ◽  
Regulated Cell Death

Insulinomimetic properties of trace elements and characterization of their in vivo mode of action

Diabetes ◽  
1990 ◽  
Vol 39 (10) ◽  
pp. 1243-1250 ◽  
Author(s):  
L. Rossetti ◽  
A. Giaccari ◽  
E. Klein-Robbenhaar ◽  
L. R. Vogel
Keyword(s):  
Trace Elements ◽  
Mode Of Action

The Study of Bacillus Subtils Antimicrobial Activity on Some of the Pathological Isolates

2019 ◽  
Vol 9 (02) ◽  
Author(s):  
Hussein A Kadhum ◽  
Thualfakar H Hasan2
Keyword(s):  
Staphylococcus Aureus ◽  
Pseudomonas Aeruginosa ◽  
Antimicrobial Activity ◽  
Bacillus Subtilis ◽  
Bacterial Growth ◽  
Broad Spectrum ◽  
Inhibitory Activity ◽  
Bacterial Pathogens ◽  
Inhibitory Ability ◽  
Selection Of

The study involved the selection of two isolates from Bacillus subtilis to investigate their inhibitory activity against some bacterial pathogens. B sub-bacteria were found to have a broad spectrum against test bacteria such as Staphylococcus aureus and Pseudomonas aeruginosa. They were about 23-30 mm and less against Klebsiella sp. The sensitivity of some antibodies was tested on the test samples. The results showed that the inhibitory ability of bacterial growth in the test samples using B. subtilis extract was more effective than the antibiotics used.

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