The role of calcium ions in the interactions of PrP106-126 amide with model membranes.

In this work, we investigated the interactions of PrP106-126 amide with 1-palmitoyl-2-oleoyl-3-phosphocholine (POPC) and POPC/bovine brain sphingomyelin (BSM) membranes in the presence of calcium ions by in situ time-lapse atomic force microscopy (AFM) and circular dichroism (CD). The CD results show that Ca2+ has no obvious effects on the random coil conformation of PrP106-126 amide. The tapping mode AFM results demonstrate that electrostatic interaction decreases the measured heights of supported lipid bilayers (SLBs) in HBS–Ca2+ solution. Electrostatic interaction analysis also can be used to determine the applied force in liquid tapping mode AFM. The interactions of PrP106-126 amide with membranes by AFM demonstrate the following: (i) Ca2+ inhibits the interaction of PrP106-126 amide with POPC lipid and (ii) the co-interaction between Ca2+ and BSM increases the poration ability of PrP106-126 amide. These results imply that the main role of Ca2+ in the interactions of PrP106-126 amide with membranes is changing the surface properties of the membranes.