Binding Orientations and Lipid Interactions of Human Amylin at Zwitterionic and Anionic Lipid Bilayers

Figure 8

Influence of membrane-bound hIAPP monomer on the tail ordering of POPC lipids. (a) Lipid tail order parameter of acyl chain 1 (sn-1). In the calculation, the lipids within 1 nm (minimum distance) from any nonhydrogen atom of hIAPP peptide are considered. We also give the of a neat POPC lipid bilayer for comparison, obtained from the last 10 ns of a 100 ns MD run. (b) Local membrane thickness for lipids within six different cutoffs from hIAPP peptide. The thickness is calculated using the average -position of the phosphorus atoms in the upper leaflet and that in the lower leaflet. The upper and lower bounds of the thickness of a neat POPC bilayer membrane ( Å) are plotted in blue dashed lines, consistent with that in [69].

(a)

(b)