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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

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.

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 Creators:
Boettcher, Christoph, Author
Kell, Henny, Author
Holzwarth, Josef F.1, Author           
Vater, Joachim, Author
Affiliations:
1Physical Chemistry, Fritz Haber Institute, Max Planck Society, ou_634546              

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Free keywords: Surfactin; Mixed DMPC–surfactin-micelles; Cryo-electron microscopy; Cryo-electron tomography
 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%.

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Language(s): eng - English
 Dates: 2010-03-16
 Publication Status: Issued
 Pages: -
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Identifiers: eDoc: 476354
DOI: 10.1016/j.bpc.2010.03.006
 Degree: -

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Title: Biophysical Chemistry
  Alternative Title : Biophys. Chem.
Source Genre: Journal
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Pages: - Volume / Issue: 149 (1-2) Sequence Number: - Start / End Page: 22 - 27 Identifier: -