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By 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.


| Dept of Biophysics | Medical Sch  | Biomed-X Center | Protein Sci CenterHealth Sci Center  | Peking Univ.

Single-molecule & Nanobiology Laboratory