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The interaction between the bacterial S-protein SbpA on different types oflipid membranes has been studied using atomic force microscopy, transmissionelectron microscopy, and quartz crystal microbalance with dissipation. On onehand, It has been found that the bacterial forms two dimensional nanocrystalson zwitterionic DOPC bilayers and negatively charged DMPG vesicles adsorbed onmica, on zwitterionic DPPC and charged DPPC/DMPG (1:1) monolayers adsorbed oncarbon grids. On the other hand, SbpA protein adsorption took place onzwitterionic DOPC bilayers and DOPC/DOPS (4:1) bilayers, previously adsorbed onsilicon supports. SbpA adsorption also took place on DPPC/DOPS (1:1) monolayersadsorbed on carbon grids. Finally, neither SbpA adsorption, norrecrystallization was observed on zwitterionic DMPC vesicles (previouslyadsorbed on polyelectrolyte multilayers), and on DPPC vesicles supported onsilicon.

On the lipid-bacterial protein interaction studied by quartz crystal  microbalance with dissipation, transmission electron microscopy and atomic  force microscopy