combination of fluorescence polarization, dye release assay and
in situ time-lapse atomic force microscopy (AFM), we
investigated the PrP106-126 amide interacting with the large
unilamellar vesicles (LUVs) and the supported lipid bilayers (SLBs).
The results suggest that the interactions involve a poration-mediated
process: firstly, the peptide binding results in the formation
of pores in the membranes, which penetrate only half of the
membranes; subsequently, PrP106-126 amide undergoes the poration-mediated
diffusion in the SLBs, represented by the formation and
expansion of the flat high-rise domains (FHDs). The possible
mechanisms of the interactions between PrP106-126 amide and
lipid membranes are proposed based on our observations.
BBA-Biomembranes 2007, by
J. Zhong, W. Zheng and et-al.