RESUMO
The structural properties of hair are largely determined by the state of the surface. Advanced imaging modes of atomic force microscopy, where the surface mechanics can be correlated with surface topography, have been used to spatially map variations in hair surfaces following chemical and mechanical treatments. Through analysis of multilayered data obtained in this way, we show that the processes of bleaching and combing of hair not only alter the surface roughness, but also alter the mechanical stiffness, adhesion properties, and surface potential of hair, in terms of the mean values and their distributions. These treatments are shown to have a significant effect on the nanoscale surface properties, consistent with what has previously been observed at the macroscopic fiber-level scale.
RESUMO
Preferential binding of F-actin to lipid bilayers containing ponticulin was investigated on both planar supported bilayers and on a cholesterol-based tethering system. The transmembrane protein ponticulin in Dictyostelium discoideum is known to provide a direct link between the actin cytoskeleton and the cell membrane ( Wuestehube, L. J. ; Luna, E. J. J. Cell Biol. 1987, 105, 1741- 1751 ). Purification of ponticulin has allowed an in vitro model of the F-actin cytoskeletal scaffold system to be formed and investigated by AFM, epi-fluorescence microscopy, surface plasmon resonance (SPR), and quartz crystal microbalance with dissipation (QCM-D). Single filament features of F-actin bound to the ponticulin containing lipid bilayer are shown by AFM to have a pitch of 37.3 +/- 1.1 nm and a filament height of 7.0 +/- 1.6 nm. The complementary techniques of QCM-D and SPR were used to obtain dissociation constants for the interaction of F-actin with ponticulin containing bilayers, giving 10.5 +/- 1.7 microM for a physisorbed bilayer and 10.8 +/- 3.6 microM for a tethered bilayer, respectively.
