Membrane lysis by gramicidin S visualized in red blood cells and giant vesicles

Semrau, Stefan; Monster, M.W.L.; Knaap, Matthijs van der; Florea, Bogdan I.; Schmidt, Thomas; Overhand, Mark

doi:10.1016/j.bbamem.2010.07.001

Cited by 20 publications

(20 citation statements)

References 41 publications

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“…Furthermore, experimentally reported bending rigidities vary based on the methods employed [136]. The three main experiments to determine bending rigidities for pure lipid bilayers are diffuse x-ray scattering of flat bilayers [43–49], force-based methods to deform a membrane such as the pipette aspiration technique and pulling membrane nanotubes [50–58,137–144], and fluctuating shape analysis of GUVs [51,59,60,145–156]. To measure the rigidity of SUVs and purified synaptic vesicles [64], neutron spin echo (NSE) [61–63], and atomic force-microscopy (AFM) experiments have been used [65–69].…”

Section: Protein-induced Alterations In Membrane Materials Propertiesmentioning

confidence: 99%

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Membrane remodeling and mechanics: Experiments and simulations of α-Synuclein

West

Brummel

Braun

et al. 2016

Biochimica et Biophysica Acta (BBA) - Biomembranes

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We review experimental and simulation approaches that have been used to determine curvature generation and remodeling of lipid bilayers by membrane-bending proteins. Particular emphasis is placed on the complementary approaches used to study α-Synuclein (αSyn), a major protein involved in Parkinson's disease (PD). Recent cellular and biophysical experiments have shown that the protein 1) deforms the native structure of mitochondrial and model membranes; and 2) inhibits vesicular fusion. Today's advanced experimental and computational technology has made it possible to quantify these protein-induced changes in membrane shape and material properties. Collectively, experiments, theory and multi-scale simulation techniques have established the key physical determinants of membrane remodeling and rigidity: protein binding energy, protein partition depth, protein density, and membrane tension. Despite the exciting and significant progress made in recent years in these areas, challenges remain in connecting biophysical insights to the cellular processes that lead to disease. This article is part of a Special Issue entitled: Membrane Proteins edited by J.C. Gumbart and Sergei Noskov.

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Section: Protein-induced Alterations In Membrane Materials Propertiesmentioning

confidence: 99%

“…Several studies used this technique to report rigidities of vesicle with added proteins [51,59,156]. In these studies, k c is extracted from thermal fluctuations in the vesicle contours.…”

Section: Protein-induced Alterations In Membrane Materials Propertiesmentioning

confidence: 99%

Membrane remodeling and mechanics: Experiments and simulations of α-Synuclein

West

Brummel

Braun

et al. 2016

Biochimica et Biophysica Acta (BBA) - Biomembranes

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“…Authors in Ref. suggested that GS did not form discrete, channel‐like stable pores; more likely, GS induces a variety of transient, differently sized defects and fast disintegration of a membrane.…”

Section: Introductionmentioning

confidence: 99%

Interaction of polypeptide antibiotic gramicidin S with platelets

Hackl

Berest

Gatash

2012

Journal of Peptide Science

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Gramicidin S (GS) is a cyclic decapeptide antibiotic active against both Gram-positive and Gram-negative bacteria as well as against several pathogenic fungi. However, clinical application of GS is limited because of GS hemolytic activity. The large number of GS analogues with potentially attenuated hemolytic activity has been developed over the last two decades. For all new GS derivatives, the antimicrobial test is accompanied with the hemolytic activity assay. At the same time, neither GS nor its analogues were tested against other blood cells. In the present work, the effects of GS on platelets and platelet aggregates have been studied. GS interaction with platelets is concentration dependent and leads either to platelet swelling or platelet shape change. Effect of GS on platelets is independent of platelet aggregation mechanism. GS induces disaggregation of platelet aggregates formed in the presence of aggregation agonists. The rate of the GS interaction with platelet membranes depends on membrane lipid mobility and significantly increases with temperature. The interaction of GS with the platelet membranes depends strongly on the state of the membrane lipids. Factors affecting the membrane lipids (temperature, lipid peroxidation and ionising irradiation) modify GS interaction with platelets. Our results show that GS is active not only against erythrocytes but also against other blood cells (platelets). The estimated numbers of GS molecules per 1 µm2 of a blood cell required to induce erythrocyte hemolysis and disaggregation of platelet aggregates are comparable. This must be considered when developing new antimicrobial GS analogues with improved hemolytic properties.

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“…In this theory, an asymmetric plasma membrane is regarded as two protein–lipid layers that are capable of performing a relatively independent adaptive deformation without losing the contact between them. The coupled bilayer theory has frequently been used to interpret the formation of echinocytes and stomatocytes under the action of membrane-active agents, including AMPs [18, 22, 23]. According to this theory, echinocyte formation is conditioned by the accumulation of the actuating agent in the external layer of the membrane.…”

Section: Resultsmentioning

confidence: 99%

N-Terminal Moiety of Antimicrobial Peptide Ltc1-K Increases its Toxicity for Eukaryotic Cells

2011

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The antimicrobial peptide Ltc1-K and its derivates without one, two, then three N-terminal amino acid residues were studied based on the hypothesis (backed by some experimental data) that the hydrophobic N-terminal moiety of linear cationic antimicrobial peptides defines their haemolytic activity. It was discovered that the excision of three N-terminal amino acid residues considerably decreases the peptide’s toxicity for eukaryotic cells and simultaneously increases the selectivity of antibacterial activity for some bacteria species. Studies performed with the model membrane systems and human erythrocytes revealed that the main reason for the observed effect is a multifold decrease in the peptide’s affinity to an eukaryotic cellular membrane enriched with zwitterionic phospholipids.

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Membrane lysis by gramicidin S visualized in red blood cells and giant vesicles

Cited by 20 publications

References 41 publications

Membrane remodeling and mechanics: Experiments and simulations of α-Synuclein

Membrane remodeling and mechanics: Experiments and simulations of α-Synuclein

Interaction of polypeptide antibiotic gramicidin S with platelets

N-Terminal Moiety of Antimicrobial Peptide Ltc1-K Increases its Toxicity for Eukaryotic Cells

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