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Originally published as Biophys J. BioFAST on May 4, 2007.
doi:10.1529/biophysj.106.101584
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Biophysical Journal 93:1608-1619 (2007)
© 2007 The Biophysical Society

Curvature-Dependent Recognition of Ethanolamine Phospholipids by Duramycin and Cinnamycin

Kunihiko Iwamoto *, Tomohiro Hayakawa {dagger}, Motohide Murate *, Asami Makino *, Kazuki Ito {ddagger}, Tetsuro Fujisawa {ddagger} and Toshihide Kobayashi * {dagger} §

* Supra-Biomolecular System Research Group, RIKEN (Institute of Physical and Chemical Research) Frontier Research System, Saitama, Japan; {dagger} Lipid Biology Laboratory, RIKEN, Saitama, Japan; {ddagger} RIKEN SPring-8 Center, Hyogo, Japan; and § INSERM UMR 870, INRA U1235, INSA-Lyon, University Lyon 1 and Hospices Civils de Lyon, Villeurbanne, France

Correspondence: Address reprint requests to Toshihide Kobayashi, Tel.: 81-48-467-9534; E-mail: kobayasi{at}riken.go.jp.

Duramycin is a 19-amino-acid tetracyclic lantibiotic closely related to cinnamycin (Ro09-0198), which is known to bind phosphatidylethanolamine (PE). The lipid specificity of duramycin was not established. The present study indicates that both duramycin and cinnamycin exclusively bind to ethanolamine phospholipids (PE and ethanolamine plasmalogen). Model membrane study indicates that the binding of duramycin and cinnamycin to PE-containing liposomes is dependent on membrane curvature, i.e., the lantibiotics bind small vesicles more efficiently than large liposomes. The binding of the lantibiotics to multilamellar liposomes induces tubulation of membranes, as revealed by electron microscopy and small-angle x-ray scattering. These results suggest that both duramycin and cinnamycin promote their binding to the PE-containing membrane by deforming membrane curvature.




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