A growing body of experimental evidence indicates that the interaction between amyloid peptide and lipid bilayer membranes plays an important role in the development of Alzheimer disease. Recent experimental evidence also suggests that trehalose, a simple disaccharide, reduces the toxicity of amyloid peptide. Molecular simulations are used to examine the effect of trehalose
on the conformational stability of amyloid peptide in aqueous solution and its effect on the interaction between amyloid peptide and a model phospholipid bilayer membrane. It is found that, in aqueous solution, the peptide exhibits a random coil conformation but, in the presence of trehalose, it adopts an alpha helical conformation. It is then shown that the insertion of amyloid peptide into a membrane is more favorable when the peptide is folded into an -helix than in a random coil conformation, thereby suggesting that trehalose promotes the insertion of -helical amyloid into biological membranes. ©2009 American Institute of Physics
Trehalose and Alzhiemers