Table 3.

Summary of molecular simulation studies focused on interactions of Aβ peptides with lipid membranes. DMPC stands for dimyristoylphosphatidyl-choline, POPC for palmitoyloleoylphosphatidylcholine, POPS for 1- palmitoyl, 2-oleoyl-sn-glycero-3-phosphoserine, and POPG for palmitoyloleoyl-phosphatidylglycerol.

References	Aβ system	Type of membrane	Simulation	Key notes
288	Aβ40 monomer	Implicit IMM1	All-atom REMD	Helical Aβ structure at membrane-water interface.
299	Aβ40 monomer	DPPC	All-atom MD	Helical Aβ structure in bilayer with tendency to exit the membrane and localize at membrane-water interface.
286	Aβ(10-40) monomer	DMPC	All-atom REMD	Helical Aβ structure at membrane-water interface.
283-285	Aβ42 monomer and dimer	DPPC and DOPS	All-atom REMD and umbrella sampling MD	Binding of Aβ to membranes. Dimerization of membrane-bound Aβ.
273,291,292	Aβ40 protofilament	POPE and POPC	All-atom MD	Interactions between Aβ fibrillar oligomers and membranes influence of lipid composition, structural effects.
300,301	Aβ40 monomer	DPPC, POPC, POPS, POPC/POPS, rafts	All-atom MD	Stability of membrane-inserted Aβ. Effect of insertion depth and membrane composition
302-304	Aβ42 dimer	Mixed bilayers with cholesterol and/or GM1 mimicking rafts	All-atom MD	Effect of rafts on membrane-binding and dimerization of Aβ.
296-298	Aβ42 monomer and oligomers	Implicit IMM1 POPC, POPG, DPPC	All-atom Monte Carlo and MD	Structure prediction for transmembrane Aβ. Testing the stability and membrane effects of the resulting β-sheet structures. Effect of mutations.
293-295	Aβ barrels	DOPC, POPC, POPG	All-atom MD	Models for Aβ channel structures. Water and ion flux across membranes through Aβ pores. Effect of Aβ mutations.
311	Aβ40 & Aβ42 monomers	3 bead model for Lipids	Coarse-grained MD	Aβ adsorption and aggregation on small vesicles