Membrane binding and pore formation of the antibacterial peptide PGLa: thermodynamic and mechanistic aspects.
about
MSI-78, an analogue of the magainin antimicrobial peptides, disrupts lipid bilayer structure via positive curvature strain.Roles of d-Amino Acids on the Bioactivity of Host Defense PeptidesOn the role of NMR spectroscopy for characterization of antimicrobial peptidesFunctional characterization of a melittin analog containing a non-natural tryptophan analogStructural Biophysics of the NusB:NusE Antitermination ComplexNMR Structures of the Histidine-Rich Peptide LAH4 in Micellar Environments: Membrane Insertion, pH-Dependent Mode of Antimicrobial Action, and DNA TransfectionDetergent-like action of the antibiotic peptide surfactin on lipid membranes.Effects of histatin 5 and derived peptides on Candida albicansMembrane-dependent oligomeric structure and pore formation of a beta-hairpin antimicrobial peptide in lipid bilayers from solid-state NMR.The thermodynamics of simple biomembrane mimetic systemsProduction of Isolated Giant Unilamellar Vesicles under High Salt Concentrations.Side chain hydrophobicity modulates therapeutic activity and membrane selectivity of antimicrobial peptide mastoparan-X.Binding of two mono-acylated lipid monomers by the barley lipid transfer protein, LTP1, as viewed by fluorescence, isothermal titration calorimetry and molecular modelling.Solution structure of a novel tryptophan-rich peptide with bidirectional antimicrobial activityMany-body effect of antimicrobial peptides: on the correlation between lipid's spontaneous curvature and pore formationProtease-stable polycationic photosensitizer conjugates between polyethyleneimine and chlorin(e6) for broad-spectrum antimicrobial photoinactivation.Activity determinants of helical antimicrobial peptides: a large-scale computational studyPore Structure and Synergy in Antimicrobial Peptides of the Magainin Family.Reorientation and dimerization of the membrane-bound antimicrobial peptide PGLa from microsecond all-atom MD simulations.Infectious Disease: Connecting Innate Immunity to Biocidal Polymers.Characterization of antibiotic peptide pores using cryo-EM and comparison to neutron scattering.Interactions of surfactants with lipid membranes.Structure and membrane interactions of the homodimeric antibiotic peptide homotarsinin.Interaction of W-substituted analogs of cyclo-RRRWFW with bacterial lipopolysaccharides: the role of the aromatic cluster in antimicrobial activity.The relationship between the binding to and permeabilization of phospholipid bilayer membranes by GS14dK4, a designed analog of the antimicrobial peptide gramicidin S.Charge-dependent translocation of the Trojan peptide penetratin across lipid membranes.Concentration-dependent realignment of the antimicrobial peptide PGLa in lipid membranes observed by solid-state 19F-NMR.Synthetic Antimicrobial Peptides Exhibit Two Different Binding Mechanisms to the Lipopolysaccharides Isolated from Pseudomonas aeruginosa and Klebsiella pneumoniae.Interactions between charged polypeptides and nonionic surfactants.Coarse-grained simulation studies of peptide-induced pore formation.Fluorescence spectroscopy in thermodynamic and kinetic analysis of pH-dependent membrane protein insertion.Influence of lipid composition on membrane activity of antimicrobial phenylene ethynylene oligomers.Energetics and partition of two cecropin-melittin hybrid peptides to model membranes of different composition.Solid-state NMR analysis of the PGLa peptide orientation in DMPC bilayers: structural fidelity of 2H-labels versus high sensitivity of 19F-NMR.A novel linear amphipathic beta-sheet cationic antimicrobial peptide with enhanced selectivity for bacterial lipids.Structures and mode of membrane interaction of a short alpha helical lytic peptide and its diastereomer determined by NMR, FTIR, and fluorescence spectroscopy.Investigation of membrane penetration depth and interactions of the amino-terminal domain of huntingtin: refined analysis by tryptophan fluorescence measurement.The application of DOSY NMR and molecular dynamics simulations to explore the mechanism(s) of micelle binding of antimicrobial peptides containing unnatural amino acids.Charged Antimicrobial Peptides Can Translocate across Membranes without Forming Channel-like Pores.Phospholipid binding of synthetic talin peptides provides evidence for an intrinsic membrane anchor of talin.
P2860
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P2860
Membrane binding and pore formation of the antibacterial peptide PGLa: thermodynamic and mechanistic aspects.
description
2000 nî lūn-bûn
@nan
2000 թուականի Յունուարին հրատարակուած գիտական յօդուած
@hyw
2000 թվականի հունվարին հրատարակված գիտական հոդված
@hy
2000年の論文
@ja
2000年論文
@yue
2000年論文
@zh-hant
2000年論文
@zh-hk
2000年論文
@zh-mo
2000年論文
@zh-tw
2000年论文
@wuu
name
Membrane binding and pore form ...... namic and mechanistic aspects.
@ast
Membrane binding and pore form ...... namic and mechanistic aspects.
@en
type
label
Membrane binding and pore form ...... namic and mechanistic aspects.
@ast
Membrane binding and pore form ...... namic and mechanistic aspects.
@en
prefLabel
Membrane binding and pore form ...... namic and mechanistic aspects.
@ast
Membrane binding and pore form ...... namic and mechanistic aspects.
@en
P2093
P356
P1433
P1476
Membrane binding and pore form ...... namic and mechanistic aspects.
@en
P2093
Apostolov O
Beyermann M
Wieprecht T
P304
P356
10.1021/BI992146K
P407
P577
2000-01-01T00:00:00Z