Collective membrane motions in the mesoscopic range and their modulation by the binding of a monomolecular protein layer of streptavidin studied by dynamic light scattering
R. Hirn et al., Collective membrane motions in the mesoscopic range and their modulation by the binding of a monomolecular protein layer of streptavidin studied by dynamic light scattering, PHYS REV E, 59(5), 1999, pp. 5987-5994
Using a dedicated dynamic light scattering setup, we have studied the angst
rom-scale amplitude undulations of freely suspended planar lipid bilayers,
so-called black lipid membranes (BLM's), over a previously not accessible s
pread of frequencies (relaxation times ranging from 10(-2) to 10(-6) s) and
wave vectors (250 cm(-1)<q<35 000 cm(-1)). This allowed a critical test of
a simple hydrodynamic theory of collective membrane modes, and the results
obtained for a synthetic lecithin BLM are found to be in excellent agreeme
nt with the theoretical predictions. In particular, the transition of the t
ransverse shear mode of a BLM between an oscillatory or propagating regime
and an overdamped regime by passing through a bifurcation point was clearly
observed. It is shown that the collective motions in the time- and wave-ve
ctor regime covered are dominated by the membrane tension, while membrane c
urvature does not contribute. The binding of the protein streptavidin to th
e BLM via membrane anchored specific binders (receptors) causes a drastic c
hange in frequency and amplitude of the collective motions, resulting in a
drastic increase of the membrane tension by a factor of 3. This effect is p
robably caused by a steric hindrance of the transverse shear motions of the
lipid by the tightly bound proteins. [S1063-651X(99)13705-X].