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)

Seung R. Paik, Ju Hyun Lee, Do Hyung Kim, Chung Soon Chang, Young Sik Kim

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63 Citations (Scopus)

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 languageEnglish
Pages (from-to)73-76
Number of pages4
JournalFEBS Letters
Volume421
Issue number1
DOIs
Publication statusPublished - 1998 Jan 2

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Keywords

  • α-Synuclein
  • Alzheimer's disease
  • Amyloid β/A4 protein fragment 25-35
  • Dicyclohexylcarbodiimide
  • Non-All component precursor
  • Oligomerization

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Molecular Biology

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