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Self‐oligomerization of NACP, the precursor protein of the non‐amyloid β/A4 protein (Aβ) component of Alzheimer's disease amyloid, observed in the presence of a C‐terminal Aβ fragment (residues 25–35)
Author(s) -
Paik Seung R,
Lee Ju-Hyun,
Kim Do-Hyung,
Chang Chung-Soon,
Kim Young-Sik
Publication year - 1998
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(97)01537-8
Subject(s) - peptide , amyloid (mycology) , chemistry , p3 peptide , c terminus , amyloid precursor protein , nucleation , biochemistry , biophysics , alzheimer's disease , amino acid , biology , medicine , disease , inorganic chemistry , pathology , organic chemistry
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.