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Preferential insertion of lactose permease in phospholipid domains: AFM observations |
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| Authors: | Laura Picas M Teresa Montero JL Vázquez-Ibar Pierre-Emmanuel Milhiet Jordi Hernández-Borrell |
| Institution: | a Departament de Fisicoquímica, Facultat de Farmàcia, Universitat de Barcelona (UB), Spain b Institut de Nanociència i Nanotecnologia de la Universitat de Barcelona (IN2UB), Spain c ICREA and Institut de Recerca Biomèdica, Parc Científic de Barcelona, 08028 Barcelona, Spain d Institut de Ciencia de Materials de Barcelona ICMAB, Consejo Superior de Investigaciones Científicas (CSIC), 08193 Bellaterra, Spain e Inserm, Unité 554, Montpellier, France f Université de Montpellier, CNRS, UMR 5048, Centre de Biochimie Structurale, Montpellier, France |
| Abstract: | 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. 7.8 nm; and (iii) keeps an area of phospholipids surrounding the protein that is compatible with shells of phospholipids. |
| Keywords: | Lactose permease AFM Phospholipid domains |
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