Preferential insertion of lactose permease in phospholipid domains: AFM observations

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Picas, Laura | Carretero-Genevrier, Adrian | Montero, M Teresa | Vázquez-Ibar, J.L. | Seantier, Bastien | Milhiet, Pierre-Emmanuel | Hernández-Borrell, Jordi | Montero, M. Teresa

Edité par CCSD ; Elsevier -

International audience. We report the insertion of a transmembrane protein, lactose permease (LacY) from Escherichia coli (E. coli), in supported lipid bilayers (SLBs) of 1-palmitoyl-2-oleoyl-sn-glycero-3-phosphoethanolamine (POPE) and 1-palmitoyl-2-oleoyl-sn-glycero-3-phosphoglycerol (POPG), in biomimetic molar proportions. We provide evidence of the preferential insertion of LacY in the fluid domains. Analysis of the self-assembled protein arrangements showed that LacY: (i) is inserted as a monomer within fluid domains of SLBs of POPE:POPG (3:1, mol/mol), (ii) has a diameter of approx. 7.8nm; and (iii) keeps an area of phospholipids surrounding the protein that is compatible with shells of phospholipids.

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