title: Adhesion-induced domain formation by interplay of long-range repulsion and short-range attraction force: a model membrane study.
abstract: We study the role of the interplay of specific and universal forces for the adhesion of giant vesicles on solid supported membranes. To model the situation of cell adhesion, we incorporated lipopolymers (phospholipids with polyethyleneoxide headgroups) as artificial glycocalix, whereas attractive lock-and-key forces are mimicked by incorporating biotinylated lipids into both membranes and by mediating the strong coupling through streptavidin. Adhesion is studied by quantitative reflection interference contrast microscopy (RICM), which enables visualization of the contact zone and reconstruction of the height profile of the membrane beyond the contact line (outside the contact zone) up to a height of 1 micron. We demonstrate that adhesion is accompanied by lateral phase separation, leading to the formation of domains of tight adhesion (adhesion plaques) separated by areas of weak adhesion exhibiting pronounced flickering. By analyzing the height profile S(x) near the contact line in terms of the tension equilibrium (Young equation) and the moment equilibrium, respectively, the adhesion energy and membrane tension can be approximately measured locally. We show that the adhesion energy is about three orders of magnitude larger for the adhesion plaques than for the weekly adhering regions. The adhesion is studied as a function of the excess area of the vesicle generated by temperature variation. A very remarkable finding is that increased excess area is not always stored in the contact area, but leads to the formation of microbuds (diameter approximately 2 microns).
authors.affiliation: Physics Department, Technische Universität München, Germany.
authors.forename: A
authors.initials: A
authors.lastname: Albersdörfer
authors.forename: T
authors.initials: T
authors.lastname: Feder
authors.forename: E
authors.initials: E
authors.lastname: Sackmann
mesh_terms: D001426:Bacterial Proteins / Q000737:chemistry*; D001665:Binding Sites; D002448:Cell Adhesion; D007700:Kinetics; D008051:Lipid Bilayers / Q000737:chemistry*; D008433:Mathematics; D008857:Microscopy, Interference; D008954:Models, Biological; D008961:Models, Structural; D010713:Phosphatidylcholines / Q000737:chemistry*; D010714:Phosphatidylethanolamines / Q000737:chemistry*; D011092:Polyethylene Glycols / Q000737:chemistry*; D017433:Protein Structure, Secondary; D019809:Streptavidin; D013314:Stress, Mechanical; D013816:Thermodynamics
chemical_list: D001426:Bacterial Proteins; D008051:Lipid Bilayers; D010713:Phosphatidylcholines; D010714:Phosphatidylethanolamines; C107332:dioleoylphosphatidylethanolamine-polyethyleneoxide; D011092:Polyethylene Glycols; D019809:Streptavidin; C017251:1,2-oleoylphosphatidylcholine