M7402

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Wall teichoic acid deficiency in Staphylococcus aureus confers selective resistance to mammalian group IIA phospholipase A(2) and human beta-defensin 3.

Tomaz Koprivnjak et al.

Infection and immunity, 76(5), 2169-2176 (2008-03-19)

Wall teichoic acids (WTAs) and membrane lipoteichoic acids (LTAs) are the major polyanionic polymers in the envelope of Staphylococcus aureus. WTAs in S. aureus play an important role in bacteriophage attachment and bacterial adherence to certain host cells, suggesting that

Magainin 2-induced pore formation in the lipid membranes depends on its concentration in the membrane interface.

Yukihiro Tamba et al.

The journal of physical chemistry. B, 113(14), 4846-4852 (2009-03-10)

Antimicrobial peptide magainin 2 forms pores in lipid membranes to induce leakage of internal contents of cells, which is a main cause of its bactericidal activity. However, the conditions and the mechanism of its pore formation remain unclear. In this

Interaction of a magainin-PGLa hybrid peptide with membranes: insight into the mechanism of synergism.

Minoru Nishida et al.

Biochemistry, 46(49), 14284-14290 (2007-11-17)

The antimicrobial peptides magainin 2 and PGLa isolated from the skin of the African clawed frog Xenopus laevis show marked functional synergism. We have proposed that the two peptides form a heterodimer composed of parallel helices with strong membrane permeabilizing

Magainins, a class of antimicrobial peptides from Xenopus skin: isolation, characterization of two active forms, and partial cDNA sequence of a precursor.

M Zasloff

Proceedings of the National Academy of Sciences of the United States of America, 84(15), 5449-5453 (1987-08-01)

A family of peptides with broad-spectrum antimicrobial activity has been isolated from the skin of the African clawed frog Xenopus laevis. It consists of two closely related peptides that are each 23 amino acids and differ by two substitutions. These

Binding of antibacterial magainin peptides to electrically neutral membranes: thermodynamics and structure.

T Wieprecht et al.

Biochemistry, 38(32), 10377-10387 (1999-08-11)

Magainins are positively charged amphiphatic peptides which permeabilize cell membranes and display antimicrobial activity. They are usually thought to bind specifically to anionic lipids, and binding studies have been performed almost exclusively with negatively charged membranes. Here we demonstrate that

Synergistic insertion of antimicrobial magainin-family peptides in membranes depends on the lipid spontaneous curvature.

Erik Strandberg et al.

Biophysical journal, 104(6), L9-11 (2013-03-27)

PGLa and magainin 2 (MAG2) are amphiphilic antimicrobial peptides from frog skin with known synergistic activity. The orientation of the two helices in membranes was studied using solid-state (15)N-NMR, for each peptide alone and for a 1:1 mixture of the

Spontaneous buckling of lipid bilayer and vesicle budding induced by antimicrobial peptide magainin 2: a coarse-grained simulation study.

Hyung-June Woo et al.

The journal of physical chemistry. B, 115(25), 8122-8129 (2011-06-10)

Molecular mechanisms of the action of antimicrobial peptides on bacterial membranes were studied by large scale coarse-grained simulations of magainin 2-dipalmitoylphosphatidylcholine/palmitoyloleoylphosphatidylglycerol (DPPC/POPG) mixed bilayer systems with spatial extents up to 0.1 μm containing up to 1600 peptides. Equilibrium simulations exhibit

Protective effects of the combination of alpha-helical antimicrobial peptides and rifampicin in three rat models of Pseudomonas aeruginosa infection.

Oscar Cirioni et al.

The Journal of antimicrobial chemotherapy, 62(6), 1332-1338 (2008-09-19)

An experimental study has been performed to compare the in vitro activity and the in vivo efficacy of magainin II and cecropin A with or without rifampicin against control and multidrug-resistant Pseudomonas aeruginosa strains. In vitro experiments included MIC determinations

In-vitro activity of cationic peptides alone and in combination with clinically used antimicrobial agents against Pseudomonas aeruginosa.

A Giacometti et al.

The Journal of antimicrobial chemotherapy, 44(5), 641-645 (1999-12-20)

The in-vitro activity of cecropin P1, indolicidin, magainin II, nisin and ranalexin alone and in combination with nine clinically used antimicrobial agents was investigated against a control strain, Pseudomonas aeruginosa ATCC 27853 and 40 clinical isolates of P. aeruginosa. Antimicrobial

Magainins as paradigm for the mode of action of pore forming polypeptides.

K Matsuzaki

Biochimica et biophysica acta, 1376(3), 391-400 (1998-11-07)

Magainins are a class of antimicrobial peptides discovered in the skin of Xenopus laevis. The peptides kill bacteria by permeabilizing the cell membranes without exhibiting significant toxicity against mammalian cells, and are a promising candidate for a new antibiotic of

In vitro activities of polycationic peptides alone and in combination with clinically used antimicrobial agents against Rhodococcus equi.

A Giacometti et al.

Antimicrobial agents and chemotherapy, 43(8), 2093-2096 (1999-08-03)

The in vitro activities of magainin II, nisin, and ranalexin alone and in combination with other antimicrobial agents against six clinical isolates of Rhodococcus equi were investigated by MIC and time-kill studies. All isolates were more susceptible to nisin. A

Magainin 2 revisited: a test of the quantitative model for the all-or-none permeabilization of phospholipid vesicles.

Sonia M Gregory et al.

Biophysical journal, 96(1), 116-131 (2009-01-13)

The all-or-none kinetic model that we recently proposed for the antimicrobial peptide cecropin A is tested here for magainin 2. In mixtures of phosphatidylcholine (PC)/phosphatidylglycerol (PG) 50:50 and 70:30, release of contents from lipid vesicles occurs in an all-or-none fashion

A critical comparison of the hemolytic and fungicidal activities of cationic antimicrobial peptides.

E J Helmerhorst et al.

FEBS letters, 449(2-3), 105-110 (1999-05-25)

The hemolytic and fungicidal activity of a number of cationic antimicrobial peptides was investigated. Histatins and magainins were inactive against human erythrocytes and Candida albicans cells in phosphate buffered saline, but displayed strong activity against both cell types when tested

Action of antimicrobial peptides: two-state model.

H W Huang

Biochemistry, 39(29), 8347-8352 (2000-07-29)

The argument and experimental evidence are presented for a two-state model that explains the action of both helical and beta-sheet antimicrobial peptides after they bind to the plasma membranes of cells. Each peptide has two distinct physical states of binding

Action mechanism of PEGylated magainin 2 analogue peptide.

Yuichi Imura et al.

Biochimica et biophysica acta, 1768(10), 2578-2585 (2007-07-31)

PEGylation is frequently used to improve the efficacy of protein and peptide drugs. Recently, we investigated its effects on the action mechanism of the cyclic beta-sheet antimicrobial peptide tachyplesin I isolated from Tachypleus tridentatus [Y. Imura, M. Nishida, Y. Ogawa

Antimicrobial peptides. A family of wound healers.

M Cannon

Nature, 328(6130), 478-478 (1987-08-06)

The cationic peptide magainin II is antimicrobial for Burkholderia cepacia-complex strains.

Joanne E Thwaite et al.

Journal of medical microbiology, 58(Pt 7), 923-929 (2009-06-09)

This study was undertaken to determine the antibacterial activity of eight cationic antimicrobial peptides towards strains of genomovars I-V of the Burkholderia cepacia complex (Bcc) in time-kill assays. All but one of the peptides failed to show activity against the

Evidence of pores and thinned lipid bilayers induced in oriented lipid membranes interacting with the antimicrobial peptides, magainin-2 and aurein-3.3.

Chul Kim et al.

Biochimica et biophysica acta, 1788(7), 1482-1496 (2009-05-05)

Dynamic structures of supramolecular lipid assemblies, such as toroidal pores and thinned bilayers induced in oriented lipid membranes, which are interacting with membrane-acting antimicrobial peptides (AMPs), magainin-2 and aurein-3.3, were explored by 31P and 2H solid-state NMR (ssNMR) spectroscopy. Various

Characterization of antibiotic peptide pores using cryo-EM and comparison to neutron scattering.

Mikyung Han et al.

Biophysical journal, 97(1), 164-172 (2009-07-08)

Magainin, a 23-residue antibiotic peptide, interacts directly with the lipid bilayer leading to cell lysis in a strongly concentration-dependent fashion. Utilizing cryo-electron microscopy, we have directly observed magainin interacting with synthetic DMPC/DMPG membranes. Visual examination shows that visibly unperturbed vesicles

Monitoring membrane binding and insertion of peptides by two-color fluorescent label.

V Y Postupalenko et al.

Biochimica et biophysica acta, 1808(1), 424-432 (2010-10-12)

Herein, we developed an approach for monitoring membrane binding and insertion of peptides using a fluorescent environment-sensitive label of the 3-hydroxyflavone family. For this purpose, we labeled the N-terminus of three synthetic peptides, melittin, magainin 2 and poly-l-lysine capable to

Antitumor activity of the antimicrobial peptide magainin II against bladder cancer cell lines.

Lehmann J

European Urology, 50(1), 141-147 (2006)

Trypanosoma cruzi: synergistic cytotoxicity of multiple amphipathic anti-microbial peptides to T. cruzi and potential bacterial hosts.

Annabeth Fieck et al.

Experimental parasitology, 125(4), 342-347 (2010-03-09)

The parasite Trypanasoma cruzi is responsible for Chagas disease and its triatomine vector, Rhodnius prolixus, has a symbiotic relationship with the soil bacterium, Rhodococcus rhodnii. R. rhodnii that was previously genetically engineered to produce the anti-microbial peptide, cecropin A was

Induction of non-lamellar lipid phases by antimicrobial peptides: a potential link to mode of action.

Evan F Haney et al.

Chemistry and physics of lipids, 163(1), 82-93 (2009-10-06)

Antimicrobial peptides are naturally produced by numerous organisms including insects, plants and mammals. Their non-specific mode of action is thought to involve the transient perturbation of bacterial membranes but the molecular mechanism underlying the rearrangement of the lipid molecules to

What determines the activity of antimicrobial and cytolytic peptides in model membranes.

Kim S Clark et al.

Biochemistry, 50(37), 7919-7932 (2011-08-30)

We previously proposed three hypotheses relating the mechanism of antimicrobial and cytolytic peptides in model membranes to the Gibbs free energies of binding and insertion into the membrane [Almeida, P. F., and Pokorny, A. (2009) Biochemistry 48, 8083-8093]. Two sets

Inducing toxicity by introducing a leucine-zipper-like motif in frog antimicrobial peptide, magainin 2.

Brijesh Kumar Pandey et al.

The Biochemical journal, 436(3), 609-620 (2011-03-26)

Cytotoxicity, a major obstacle in therapeutic application of antimicrobial peptides, is controlled by leucine-zipper-like sequences in melittin and other naturally occurring antimicrobial peptides. Magainin 2 shows significantly lower cytotoxicity than many naturally occurring antimicrobial peptides and lacks this structural element.

Distribution of BODIPY-labelled phosphatidylethanolamines in lipid bilayers exhibiting different curvatures.

Radek Šachl et al.

Physical chemistry chemical physics : PCCP, 13(24), 11694-11701 (2011-05-21)

In this paper we have investigated the behaviour of newly synthesised mono-palmitoyl- and dipalmitoyl-phosphatidylethanolamine probes (abbreviated as mPE and dPE, respectively) labelled in the polar headgroup region by either the FL-BODIPY or the 564/570-BODIPY fluorophore and solubilised in lipid systems

The cytotoxic effect of magainin II on the MDA-MB-231 and M14K tumour cell lines.

Anghel R

BioMed Research International, 2013:831709 (2013)

Synergistic transmembrane insertion of the heterodimeric PGLa/magainin 2 complex studied by solid-state NMR.

Erik Strandberg et al.

Biochimica et biophysica acta, 1788(8), 1667-1679 (2009-03-11)

The skin secretions of amphibians are a rich source of antimicrobial peptides. The two antimicrobial peptides PGLa and magainin 2, isolated from the African frog Xenopus laevis, have been shown to act synergistically by permeabilizing the membranes of microorganisms. In

Antimicrobial peptide P18 inhibits inflammatory responses by LPS- but not by IFN-gamma-stimulated macrophages.

Yong Hai Nan et al.

Biotechnology letters, 30(7), 1183-1187 (2008-03-11)

Antimicrobial peptide P18 markedly inhibited the expression of inducible nitric oxide synthase (iNOS), tumor necrosis factor-alpha (TNF-alpha) and interleukin-1 beta (IL-1beta) in lipopolysaccharide (LPS)-stimulated RAW264.7 macrophage cells, whereas magainin 2 did not inhibit these activities. P18 dose-dependently reduced nitric oxide

Magainin 2 in action: distinct modes of membrane permeabilization in living bacterial and mammalian cells.

Imura Y

Biophysical Journal, 95(12), 5757-5765 (2008)

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