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  Vesicle adhesion and fusion studied by small-angle x-ray scattering.

Komorowski, K., Salditt, A., Xu, Y., Yavuz, H., Brennich, M., Jahn, R., et al. (2018). Vesicle adhesion and fusion studied by small-angle x-ray scattering. Biophysical Journal, 114(8), 1908-1920. doi:10.1016/j.bpj.2018.02.040.

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Item Permalink: http://hdl.handle.net/21.11116/0000-0001-3BED-3 Version Permalink: http://hdl.handle.net/21.11116/0000-0003-79B5-9
Genre: Journal Article

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 Creators:
Komorowski, K.1, Author              
Salditt, A., Author
Xu, Y., Author
Yavuz, H.1, Author              
Brennich, M., Author
Jahn, R.1, Author              
Salditt, T., Author
Affiliations:
1Department of Neurobiology, MPI for Biophysical Chemistry, Max Planck Society, ou_578595              

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 Abstract: We have studied the adhesion state (also denoted by docking state) of lipid vesicles as induced by the divalent ions Ca2+ or Mg2+ at well-controlled ion concentration, lipid composition, and charge density. The bilayer structure and the interbilayer distance in the docking state were analyzed by small-angle x-ray scattering. A strong adhesion state was observed for DOPC:DOPS vesicles, indicating like-charge attraction resulting from ion correlations. The observed interbilayer separations of ∼1.6 nm agree quantitatively with the predictions of electrostatics in the strong coupling regime. Although this phenomenon was observed when mixing anionic and zwitterionic (or neutral) lipids, pure anionic membranes (DOPS) with highest charge density σ resulted in a direct phase transition to a multilamellar state, which must be accompanied by rupture and fusion of vesicles. To extend the structural assay toward protein-controlled docking and fusion, we have characterized reconstituted N-ethylmaleimide-sensitive factor attachment protein receptors in controlled proteoliposome suspensions by small-angle x-ray scattering.

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Language(s): eng - English
 Dates: 2018-04-252018-04-24
 Publication Status: Published in print
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 Rev. Method: Peer
 Identifiers: DOI: 10.1016/j.bpj.2018.02.040
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Title: Biophysical Journal
Source Genre: Journal
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Pages: - Volume / Issue: 114 (8) Sequence Number: - Start / End Page: 1908 - 1920 Identifier: -