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M7402
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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
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
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
Antimicrobial peptides. A family of wound healers.
M Cannon
Nature, 328(6130), 478-478 (1987-08-06)
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
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
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
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
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
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
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
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
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
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
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
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
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
Clarisse Bourbon et al.
Analytical biochemistry, 381(2), 279-281 (2008-07-29)
Antimicrobial peptides are good leads to develop new antibiotics, but knowledge of their mode of action is a prerequisite. Destruction of the microbial membranes through a detergent-like mechanism is one of these modes of action. This is usually studied by
Khoi Tan Nguyen et al.
The journal of physical chemistry. B, 113(36), 12358-12363 (2009-09-05)
In this paper, we investigated the molecular interactions of magainin 2 with model cell membranes using sum frequency generation (SFG) vibrational spectroscopy and attenuated total reflectance-Fourier transform infrared spectroscopy (ATR-FTIR). Symmetric 1-palmitoyl-2-oleoyl-sn-glycero-3-[Phospho-rac-(1-glycerol)] (POPG) and 1-palmitoyl-2-oleoyl-sn-glycero-3-phosphocholine (POPC) bilayers, which model the
Magainin 2 in action: distinct modes of membrane permeabilization in living bacterial and mammalian cells.
Imura Y
Biophysical Journal, 95(12), 5757-5765 (2008)
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
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
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
The cytotoxic effect of magainin II on the MDA-MB-231 and M14K tumour cell lines.
Anghel R
BioMed Research International, 2013:831709 (2013)
A carpet-based mechanism for direct antimicrobial peptide activity against vaccinia virus membranes.
R E Dean et al.
Peptides, 31(11), 1966-1972 (2010-08-14)
Antimicrobial peptides have activity against a wide variety of biological membranes and are an important component of innate immunity in vertebrate as well as invertebrate systems. The mechanisms of action of these peptides are incompletely understood and a number of
Yeu-Chun Kim et al.
Journal of controlled release : official journal of the Controlled Release Society, 122(3), 375-383 (2007-07-14)
In this study we tested the hypothesis that magainin, a peptide known to form pores in bacterial cell membranes, can increase skin permeability by disrupting stratum corneum lipid structure. We further hypothesized that magainin's enhancement requires co-administration with a surfactant
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
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)
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
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