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NEW Study reveals How Trehalose Causes Positive Brain Membrane Interaction in Alzheimer’s Disease
NEW Trehalose Study reveals How Trehalose Causes Positive Brain Membrane Interaction in Alzheimer’s Disease

Comments by J. C. Spencer

New research suggests HOW the disaccharide trehalose reduces the toxicity of the amyloid β peptide. Evidence indicated that it is this amyloid β toxicity that plays an important role in the development of Alzheimer’s disease. Trehalose actually appears to fold the peptide favorably. Trehalose promotes the insertion of α-helical amyloid β into biological membranes.

The Endowment for Medical Research in Houston continues its Trehalose Pilot Surveys so as to gather evaluation reports from neurodegenerative challenges. The Evaluation Forms may be downloaded from the website at www.endowmentmed.org

Now for the Abstract.

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Effect of trehalose on amyloid (29–40)-membrane interaction

J. Chem. Phys. 131, 085101 (2009); doi:10.1063/1.3193726
Published 24 August 2009

ABSTRACT
REFERENCES (50)

Allam S. Reddy, Aslin Izmitli, and J. J. de Pablo
Department of Chemical Engineering, University of Wisconsin, Madison, Wisconsin 53706-1691, USA

A growing body of experimental evidence indicates that the interaction between amyloid β 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 β peptide. Molecular simulations are used to examine the effect of trehalose on the conformational stability of amyloid β peptide in aqueous solution and its effect on the interaction between amyloid β 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 β 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 β into biological membranes. ©2009 American Institute of Physics

AIP: The Journal of Chemical Physics

www.endowmentmed.org

Last Updated ( Sep 03, 2009 at 10:53 AM )