N-terminal truncated pyroglutamyl β amyloid peptide Aβpy3-42 shows a faster aggregation kinetics than the full-length Aβ1-42
✍ Scribed by Cristina D'Arrigo; Massimo Tabaton; Angelo Perico
- Publisher
- Wiley (John Wiley & Sons)
- Year
- 2009
- Tongue
- English
- Weight
- 446 KB
- Volume
- 91
- Category
- Article
- ISSN
- 0006-3525
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✦ Synopsis
Abstract
We tested directly the differences in the aggregation kinetics of three important β amyloid peptides, the full‐length Aβ1‐42, and the two N‐terminal truncated and pyroglutamil modified Aβ__py__3‐42 and Aβ__py__11‐42 found in different relative concentrations in the brains in normal aging and in Alzheimer disease. By following the circular dichroism signal and the ThT fluorescence of the solution in phosphate buffer, we found substantially faster aggregation kinetics for Aβ__py__3‐42. This behavior is due to the particular sequence of this peptide, which is also responsible for the specific oligomeric aggregation states, found by TEM, during the fibrillization process, which are very different from those of Aβ1‐42, more prone to fibril formation. In addition, Aβ__py__3‐42 is found here to have an inhibitory effect on Aβ1‐42 fibrillogenesis, coherently with its known greater infective power. This is an indication of the important role of this peptide in the aggregation process of β‐peptides in Alzheimer disease. © 2009 Wiley Periodicals, Inc. Biopolymers 91: 861–873, 2009.
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