S-layer reconstitution at phospholipid monolayers

Autor: Mathias Lösche, E. Györvary, Uwe B. Sleytr, A. Pfandler, Dietmar Pum, B. Wetzer
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Zdroj: Scopus-Elsevier
Popis: The recrystallization of the S-layer protein from Bacillus coagulans E38-66 at different lipid surface monolayer films has been observed to depend on (i) the nature of the lipid headgroup, (ii) the phase state of the surface monolayer, (iii) the ionic content, and (iv) the pH of the subphase. S-layer lattices formed at such interfaces were studied by electron microscopy and their orientation with respect to the lipid films was determined from the handedness ofthe base vectors defining the oblique crystal lattice. Recrystallization of S-layer lattices that cover the entire sample area was generally observed at lipids with zwitterionic headgroups in the presence of Ca 2+ if the lipid chains possessed a high degree of order, i.e., if the lipid film was in the liquid condensed phase. Under such conditions, the S-layer was found to be attached to the lipid with its net negatively charged inner face. In contrast, the S-layer protein recrystallized poorly under most lipids with negatively charged headgroups and under lipids with unsaturated chains. At monolayers of cationic lipids, reconstituted S-layers were observed in which the protein was attached to the liDid with its outer face.
Databáze: OpenAIRE