The interaction of phospholipase A2 with a phospholipid bilayer: coarse-grained molecular dynamics simulations.

摘要: A number of membrane-active enzymes act in a complex environment formed by the interface between lipid bilayer and bulk water. Although x-ray diffraction studies yield structures isolated enzyme molecules, detailed characterization their interactions with requires measure how deeply such membrane-associated protein penetrates into bilayer. Here, we apply coarse-grained (CG) molecular dynamics (MD) simulations to probe interaction porcine pancreatic phospholipase A2 (PLA2) containing palmitoyl-oleoyl-phosphatidyl choline glycerol molecules. We also used configuration from CG-MD trajectory initiate two atomistic (AT) MD simulations. The results CG AT are evaluated comparison available experimental data. membrane-binding surface PLA2 consists patch hydrophobic residues surrounded polar basic residues. show this proposed footprint interacts preferentially anionic headgroups Thus, both electrostatic determine location relative From general perspective, study demonstrates that may be reveal orientation membrane-surface-bound bilayer, which subsequently refined AT-MD more interactions.