In Silico Analysis of the Apolipoprotein E and the Amyloid β Peptide Interaction: Misfolding Induced by Frustration of the Salt Bridge Network
Figure 3
Distance analysis between ApoE residues involved in the electrostatic interactions between helices II and III of the N-terminal domain during the ApoE-Aβ complex formation.
The structure plotted corresponds to the ApoE4-Aβ complex (color code blue and golden, respectively). The sub index for the ApoE4 residues indicates helix location. The green dotted line depicts the salt bridge network between residues in the ApoE4 helices II and III. (A) Distance variation during the 10 ns MD simulation for the Arg61-Glu66 electrostatic pair, for ApoE4 alone (grey) and for ApoE4-Aβ (black). (B) Distance variation during the 10 ns MD simulation for the Arg61-Glu109 electrostatic pair, for ApoE4 alone (grey) and for ApoE4-Aβ (black). (C) Distance variation during the 10 ns MD simulation for the Arg112-Glu109 electrostatic pair, for ApoE4 alone (grey) and for ApoE4-Aβ (black). (D) Distance variation during the 10 ns MD simulation for the Arg112-Asp110 electrostatic pair, for ApoE4 alone (grey) and for ApoE4-Aβ (black). In all plots the salt bridge thresholds of 4.3 and 7.0 Å are indicated by dashed lines. Selected residues have been represented as ball and sticks and colored by element (C, grey; O, red; N, blue).