A quantitative model for the all-or-none permeabilization of phospholipid vesicles by the antimicrobial peptide cecropin A.
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A chaotic pore model of polypeptide antibiotic actionOn the role of NMR spectroscopy for characterization of antimicrobial peptidesTime-resolved fluorescence in lipid bilayers: selected applications and advantages over steady stateStructure and Membrane Interactions of the Antibiotic Peptide Dermadistinctin K by Multidimensional Solution and Oriented 15N and 31P Solid-State NMR SpectroscopyPhosphatidylethanolamine binding is a conserved feature of cyclotide-membrane interactions.Localized permeabilization of E. coli membranes by the antimicrobial peptide Cecropin A.Biomolecular engineering by combinatorial design and high-throughput screening: small, soluble peptides that permeabilize membranes.α-helical structures drive early stages of self-assembly of amyloidogenic amyloid polypeptide aggregate formation in membranes.Effect of extracted housefly pupae peptide mixture on chilled pork preservation.Additive and synergistic membrane permeabilization by antimicrobial (lipo)peptides and detergentsAntimicrobial peptides bind more strongly to membrane poresMembrane-active peptides: binding, translocation, and flux in lipid vesicles.Lysylated phospholipids stabilize models of bacterial lipid bilayers and protect against antimicrobial peptides.Mathematical modeling of K-Ras nanocluster formation on the plasma membrane.Broad-spectrum antimicrobial peptides by rational combinatorial design and high-throughput screening: the importance of interfacial activity.Lysyl-phosphatidylglycerol attenuates membrane perturbation rather than surface association of the cationic antimicrobial peptide 6W-RP-1 in a model membrane system: implications for daptomycin resistance.Describing the mechanism of antimicrobial peptide action with the interfacial activity modelProbing membrane topology of the antimicrobial peptide distinctin by solid-state NMR spectroscopy in zwitterionic and charged lipid bilayers.Peptides with the same composition, hydrophobicity, and hydrophobic moment bind to phospholipid bilayers with different affinities.Biphasic effects of insulin on islet amyloid polypeptide membrane disruption.A thermodynamic approach to the mechanism of cell-penetrating peptides in model membranesA lipocentric view of peptide-induced pores.Islet amyloid polypeptide demonstrates a persistent capacity to disrupt membrane integrityWhat determines the activity of antimicrobial and cytolytic peptides in model membranesStructure and function of papiliocin with antimicrobial and anti-inflammatory activities isolated from the swallowtail butterfly, Papilio xuthus.Hemolytic activity of membrane-active peptides correlates with the thermodynamics of binding to 1-palmitoyl-2-oleoyl-sn-glycero-3-phosphocholine bilayersCommon mechanism unites membrane poration by amyloid and antimicrobial peptides.Kinetics of endophilin N-BAR domain dimerization and membrane interactions.The activity of the amphipathic peptide delta-lysin correlates with phospholipid acyl chain structure and bilayer elastic properties.Statistical analysis of peptide-induced graded and all-or-none fluxes in giant vesiclesA common landscape for membrane-active peptides.Lipid composition-dependent membrane fragmentation and pore-forming mechanisms of membrane disruption by pexiganan (MSI-78)Magainin 2 revisited: a test of the quantitative model for the all-or-none permeabilization of phospholipid vesicles.Interactions of surfactants with lipid membranes.Wasp mastoparans follow the same mechanism as the cell-penetrating peptide transportan 10.Mechanisms of antimicrobial, cytolytic, and cell-penetrating peptides: from kinetics to thermodynamics.Translocation of cationic amphipathic peptides across the membranes of pure phospholipid giant vesicles.Antimicrobial peptides: successes, challenges and unanswered questions.Insights into the mechanisms of action of host defence peptides from biophysical and structural investigations.Membrane-active host defense peptides--challenges and perspectives for the development of novel anticancer drugs.
P2860
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P2860
A quantitative model for the all-or-none permeabilization of phospholipid vesicles by the antimicrobial peptide cecropin A.
description
2007 nî lūn-bûn
@nan
2007年の論文
@ja
2007年学术文章
@wuu
2007年学术文章
@zh-cn
2007年学术文章
@zh-hans
2007年学术文章
@zh-my
2007年学术文章
@zh-sg
2007年學術文章
@yue
2007年學術文章
@zh
2007年學術文章
@zh-hant
name
A quantitative model for the a ...... imicrobial peptide cecropin A.
@ast
A quantitative model for the a ...... imicrobial peptide cecropin A.
@en
type
label
A quantitative model for the a ...... imicrobial peptide cecropin A.
@ast
A quantitative model for the a ...... imicrobial peptide cecropin A.
@en
prefLabel
A quantitative model for the a ...... imicrobial peptide cecropin A.
@ast
A quantitative model for the a ...... imicrobial peptide cecropin A.
@en
P2093
P2860
P1433
P1476
A quantitative model for the a ...... timicrobial peptide cecropin A
@en
P2093
Allison Cavenaugh
Antje Pokorny
Paulo F F Almeida
Sonia M Gregory
P2860
P304
P356
10.1529/BIOPHYSJ.107.118760
P407
P577
2007-10-05T00:00:00Z