Alzheimer Disease

Human amyloid-b peptide 1-42 (Ab) was subjected to a radical reaction using ascorbic acid and CuCl2. At 24 h the percentage of D-aspartic acid (D-Asp) increased to 6.69 ± 0.09%, which was comparable with the reported D-Asp concentration of purified core amyloids of Alzheimer’s disease patients (Tambo et al, 2013). This racemization was significantly inhibited by radical scavengers. The racemization of Asp by a radical reaction is much faster than that by an ionic reaction. L-Alanine was also racemized during the same reaction. (Tambo et al, 2013)


  • K. Tambo, T. Yamaguchi, K. Kobayashi, E. Terauchi, I. Ichi, and S. Kojo. Racemization of the aspartic acid residue of amyloid-b peptide by a radical reaction. Biosci. Biotechnol. Biochem., 77, 416-418 (2013)


  • Shosuke Kojo, Nara Women's University