Journal
FEBS LETTERS
Volume 579, Issue 17, Pages 3574-3578Publisher
WILEY
DOI: 10.1016/j.febslet.2005.05.036
Keywords
Alzheimer's disease; charge substitution; net charge; A beta 40; oligomerization
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The strong pH dependence of A beta oligomerization could arise from favorable intermolecular charge-charge interactions between His and carboxylate groups, or, alternatively, by mutual electrostatic repulsion of peptide molecules. To test between these two possibilities, the pH dependence of the oligomerization of A beta and three charge substitution variants with Asp, Glu and His substituted by Ala is measured. All four peptides oligomerize, as detected by thioflavin T fluorescence, turbidity, and amyloid fibril formation; therefore, specific charge-charge interactions are nonessential for oligomerization. The strong negative correlation between net charge and oligomerization indicates that electrostatic repulsion between A beta monomers impedes their association. (c) 2005 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.
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