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Flexible loops of thread-like micelles are formed upon interaction of L-α-dimyristoyl-phosphatidyl-choline with the biosurfactant surfactin as revealed by cryo-electron tomography

Vesicles of L-α-dimyristoyl phosphatidylcholine (DMPC) are known to disintegrate upon treatment with surfactin, a lipoheptapeptide biosurfactant from Bacillus subtilis OKB 105 as was observed by static light scattering (SLS) and cryo-transmission electron microscopy (cryo-TEM) recently. The lysis of DMPC bilayers occurs strongly dependent on the surfactin concentration according to a three-stage model. Unilamellar DMPC-vesicles are disrupted to form sheet-like lamellar intermediates at a moderate surfactant concentration, but undergo a transition towards smaller particles of unknown structure at a higher surfactant concentration according to earlier neutron scattering experiments. Here we present direct structural evidence from cryo-electron tomography data that thread-like micelles...

Autoren:   Christoph, Boettcher , Henny, Kell , Josef F., Holzwarth , Joachim, Vater
Journal:   Biophysical Chemistry
Jahrgang:   2010
DOI:   10.1016/j.bpc.2010.03.006
Erscheinungsdatum:   17.03.2010
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