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

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Holzwarth,  Josef F.
Physical Chemistry, Fritz Haber Institute, Max Planck Society;

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Citation

Boettcher, C., Kell, H., Holzwarth, J. F., & Vater, J. (2010). Flexible loops of thread-like micelles are formed upon interaction of L-α-dimyristoyl-phosphatidylcholine with the biosurfactant surfactin as revealed by cryo-electron tomography. Biophysical Chemistry, 149(1-2), 22-27. doi:10.1016/j.bpc.2010.03.006.


Cite as: https://hdl.handle.net/11858/00-001M-0000-0010-F604-E
Abstract
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 cryoelectron tomography data that thread-like micelles with a uniform diameter of 6.5 nmare organized into loops of different sizes at a surfactin concentration of >15 mol%.