Abstract
NACP, the precursor protein of the non-amyloid β/A4 protein (Aβ) component of Alzheimer's disease (AD) amyloid, also known as α-synuclein, was suggested to seed amyloid plaque formation in AD by stimulating Aβ aggregation. We have demonstrated that NACP experienced self-oligomerization only in the presence of a modified Aβ fragment (Aβ25-35) by using dicyclohexylcarbodiimide. This NACP oligomerization, appearing as a discrete ladder on a Tricine SDS-PAGE, was not observed with other Aβ peptides such as the reverse peptide Aβ35-25 and Aβ1-40, indicating this process was specific not only for the C-terminal peptide sequence of the Aβ but also for its orientation. It might be, therefore, suggested that the NACP self- oligomers formed only in the presence of a N-terminally truncated Aβ peptide could act as a nucleation center for plaque formation during AD development.
Original language | English |
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Pages (from-to) | 73-76 |
Number of pages | 4 |
Journal | FEBS Letters |
Volume | 421 |
Issue number | 1 |
DOIs | |
Publication status | Published - 1998 Jan 2 |
Keywords
- Alzheimer's disease
- Amyloid β/A4 protein fragment 25-35
- Dicyclohexylcarbodiimide
- Non-All component precursor
- Oligomerization
- α-Synuclein
ASJC Scopus subject areas
- Biophysics
- Structural Biology
- Biochemistry
- Molecular Biology
- Genetics
- Cell Biology