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surfactin peptide and dimyristoylphosphatidylcholine

surfactin peptide has been researched along with dimyristoylphosphatidylcholine in 4 studies

Research

Studies (4)

TimeframeStudies, this research(%)All Research%
pre-19900 (0.00)18.7374
1990's1 (25.00)18.2507
2000's2 (50.00)29.6817
2010's1 (25.00)24.3611
2020's0 (0.00)2.80

Authors

AuthorsStudies
Maget-Dana, R; Ptak, M1
Boettcher, C; Heenan, RK; Holzwarth, JF; Kell, H; Vater, J1
Besson, F; Brisson, A; Buchoux, S; Dufourc, EJ; Garnier, M; Lai-Kee-Him, J; Tsan, P1
Boettcher, C; Holzwarth, JF; Kell, H; Vater, J1

Other Studies

4 other study(ies) available for surfactin peptide and dimyristoylphosphatidylcholine

ArticleYear
Interactions of surfactin with membrane models.
    Biophysical journal, 1995, Volume: 68, Issue:5

    Topics: 1,2-Dipalmitoylphosphatidylcholine; Amino Acid Sequence; Aniline Compounds; Antibiotics, Antineoplastic; Bacillus subtilis; Bacterial Proteins; Cholesterol; Circular Dichroism; Dimyristoylphosphatidylcholine; Lipopeptides; Liposomes; Molecular Conformation; Molecular Sequence Data; Peptides, Cyclic; Phosphatidylcholines; Phosphatidylethanolamines; Phosphatidylserines; Protein Conformation; Structure-Activity Relationship

1995
Physicochemical studies of the interaction of the lipoheptapeptide surfactin with lipid bilayers of L-alpha-dimyristoyl phosphatidylcholine.
    Biophysical chemistry, 2007, Volume: 128, Issue:2-3

    Topics: Calorimetry, Differential Scanning; Dimyristoylphosphatidylcholine; Light; Lipid Bilayers; Lipopeptides; Microscopy, Electron; Molecular Structure; Peptides, Cyclic; Phase Transition; Temperature

2007
Surfactin-triggered small vesicle formation of negatively charged membranes: a novel membrane-lysis mechanism.
    Biophysical journal, 2008, Volume: 95, Issue:8

    Topics: Dimyristoylphosphatidylcholine; Hydrogen-Ion Concentration; Lipid Bilayers; Lipopeptides; Liposomes; Magnetic Resonance Spectroscopy; Microscopy, Electron, Transmission; Models, Biological; Peptides, Cyclic; Phosphatidylglycerols; Temperature

2008
Flexible loops of thread-like micelles are formed upon interaction of L-alpha-dimyristoyl-phosphatidylcholine with the biosurfactant surfactin as revealed by cryo-electron tomography.
    Biophysical chemistry, 2010, Volume: 149, Issue:1-2

    Topics: Computer Simulation; Cryoelectron Microscopy; Dimyristoylphosphatidylcholine; Lipopeptides; Micelles; Peptides, Cyclic; Protein Structure, Tertiary; Surface-Active Agents; Unilamellar Liposomes

2010