A. Raudino et al., Binding of lipid vesicles to protein-coated solid polymer surfaces: A model for cell adhesion to artificial biocompatible materials, J COLL I SC, 231(1), 2000, pp. 66-73
The adhesion of lipid vesicles (liposomes) having controlled chemical and p
hysical structure to polymer supported human serum albumin (HSA) thin layer
s was investigated by a spectrofluorimetric technique. The vesicle lipid bi
layer was labeled with a small amount of an apolar fluorescent probe (diphe
nylexathriene) and the vesicle suspension was set in contact with the prote
in film. After washing and drying, the adhering vesicles containing sample
was dissolved in chloroform and the homogeneous solution was analyzed by st
andard spectrofluorimetric techniques. Different parameters of the lipid bi
layer, suspending solution, and protein film were varied and their influenc
e on the liposome binding was investigated. Concerning the lipid bilayer, w
e studied the effect of liposome surface charge by using different mixtures
of neutral (dipalmitoyl-phosphatidylcholine) and charged (dipalmitoyl-phos
phatidic acid) phospholipids and the fluid or gel nature of the lipid bilay
er (switched on and off by temperature variation). Variations of the local
environment involve Ca2+ and H+ changes in the millimolar range as well as
different hydrodynamical flows (in the range 0.1-10 cm/s). Preliminary meas
urements using different protein layers were also performed. Results show:
(a) negligible adhesion without the protein layer, (b) the presence of a ma
ximum for the liposome adhesion vs ion concentration (depending on the lipo
some composition and kind of the adsorbed ions), (c) a much stronger adhesi
on for vesicles in the fluid phase (overcoming the entropy-driven desorptio
n increase with temperature), and (d) a dramatic lowering of the adhesion c
apability under hydrodynamic flow. Points a-e have been interpreted on the
basis of a simple mechanoelectrical model. (C) 2000 Academic Press.