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2005:
Guo Meng; Gorman Paul M; Rico Manuel; Chakrabartty Avijit; Laurents Douglas V
Charge substitution shows that repulsive electrostatic interactions impede the oligomerization of Alzheimer amyloid peptides.
FEBS letters 2005;
579(
17):.
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.
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