Effect Of Trehalose On Alzheimer's Amyloid Beta (1-40) - Membrane Interaction

Tuesday, November 6, 2007 - 9:44 AM
205e

Effect Of Trehalose On Alzheimer's Amyloid Beta (1-40) - Membrane Interaction

Allam S. Reddy¹, Aslin Izmitli¹, Carolina Schebor², and Juan J. De Pablo³. (1) Department of Chemical and Biological Engineering, University of Wisconsin-Madison, 1415 Engineering Drive, Madison, WI 53706-1691, (2) Facultad de Ciencias Exactas y Naturales, Departmento de Industrias,, Universidad de Buenos Aires, Ciudad Universitaria (1428), Ciudad Universitaria, Buenos Aires, Argentina, (3) Chemical and Biological Engineering, University of Wisconsin-Madison, 1415 Engineering Drive, Madison, WI 53706

The interaction of amyloid β-protein with cell membranes is believed to play a central role in the pathogenisis of Alzheimer's disease (AD). Understanding that interaction could lead to the development of therapeutics for treating AD. Trehalose, a disaccharide of glucose, has been shown to be effective in preventing the aggregation of numerous proteins and in protecting cells against stress. Using Langmuir isotherms, fluorescence microscopy, and atomic force microscopy we study the kinetics of insertion of Aβ peptide into DPPG monolayers in water and in a trehalose subphase. We show that in water subphase, the insertion of the Aβ peptide into the membrane exhibits a lag time which decreases with increasing temperature of the subphase. In the presence of trehalose, the lag time is completly eliminated and peptide insertion is completed within a shorter time period compared to water subphase. Also at long times, the inserted peptide under the water subphase undergoes considerable aggregation. In contrast, in the presence of trehalose, no aggregation occurs within the time of observation.

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