Amyloid-beta peptide A beta p3-42 affects early aggregation of full-length A beta 1-42
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Date
2009-05
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Authors
Sanders, Hiromi M.
Lust, Robert M.
Teller, Jan K.
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Publisher
East Carolina University
Abstract
The major amyloid beta (Aβ) peptides found in the brain of familial and late onset Alzheimer’s
disease include the full-length Aβ1-42 and N-terminally truncated, pyroglutamylated peptides
Aβp3-42 and Aβp11-42. The biophysical properties of Aβ1-42 have been extensively studied, yet
little is known about the other modified peptides. We investigated the aggregation kinetics of brainspecific
Aβ peptides to better understand their potential roles in plaque formation. Synthetic peptides
were analyzed individually and in mixtures representing various ratios found in the brain.
Spectrofluorometric analyses using Thioflavin-T showed that the aggregation of Aβ1-42 was faster
compared to Aβp3-42; however, Aβp11-42 displayed similar kinetics. Surprisingly, mixtures of fulllength
Aβ1-42 and Aβp3-42 showed an initial delay in beta-sheet formation from both equimolar
and non-equimolar samples. Electron microscopy of peptides individually and in mixtures further
supported fluorescence data. These results indicate that Aβ-Aβ peptide interactions involving
different forms may play a critical role in senile plaque formation and maintenance of the soluble
Aβ pool in the brain. Originally published Peptides, Vol. 30, No. 5, May 2009
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Citation
Peptides; 30:5 p. 849-854
DOI
10.1016/j.peptides.2009.01.027