Figure 4
From: Complex approach for analysis of snake venom α-neurotoxins binding to HAP, the high-affinity peptide
Molecular dynamics analisys of putative complexes between peptide HAP[L9E] (most efficiently binding αCtx) and neurotoxins αCtx and αBgt. (A,B) complexes of αBgt and αCtx with HAP[L9E] after 200 ns of MD. Polypeptide chains are shown as a ribbon; αBgt coloured in red, αCtx – in green, HAP[L9E] – in grey; yellow sticks show disulfide bridges. Cyan sticks show HAP[L9E] residue Glu9; pink sticks show α-neurotoxins residues Arg36/Arg33; nitrogen and oxygen atoms are shown in blue and red, respectively; yellow dashed lines show intermolecular contacts. (C) Interaction energy profiles of HAP/HAP[L9E] in complex with αBgt and αCtx. The bar chart shows amino acid residues’ contributions to the interaction energy averaged over MD simulation. Error bars indicate standard deviations. Glu9 makes a positive impact (negative energy contribution), while Leu9 impact is negligible. All drawings showing 3D structures were prepared with the PyMOL Molecular Graphics System, version 1.8 (The PyMOL Molecular Graphics System, Version 1.8 Schrödinger, LLC; https://pymol.org/2/).
