Racemization of the Aspartic Acid Residue of Amyloid-β Peptide by a Radical Reaction

Human amyloid-β peptide 1-42 (Aβ) was subjected to a radical reaction by using ascorbic acid and CuCl(2). The percentage of D-aspartic acid (D-Asp) after 24 h had increased to 6.69 ± 0.09%, this being comparable with the reported D-Asp concentration of purified core amyloids in Alzheimer's dise...

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Bibliographic Details
Published in:Bioscience, biotechnology, and biochemistry biotechnology, and biochemistry, 2013, Vol.77 (2), p.416-418
Main Authors: TAMBO, Koharu, YAMAGUCHI, Tomomi, KOBAYASHI, Keiko, TERAUCHI, Eri, ICHI, Ikuyo, KOJO, Shosuke
Format: Article
Language:English
Subjects:
Alzheimer's disease
amyloid
Amyloid beta-Peptides - chemistry
Ascorbic Acid - chemistry
Aspartic Acid - chemistry
Chromans - chemistry
Copper - chemistry
D-aspartic acid
Free Radical Scavengers - chemistry
Free Radicals - antagonists & inhibitors
Humans
Mercaptoethanol - chemistry
Peptide Fragments - chemistry
racemization
radical
Solutions
Stereoisomerism
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Summary:Human amyloid-β peptide 1-42 (Aβ) was subjected to a radical reaction by using ascorbic acid and CuCl(2). The percentage of D-aspartic acid (D-Asp) after 24 h had increased to 6.69 ± 0.09%, this being comparable with the reported D-Asp concentration of purified core amyloids in Alzheimer's disease patients. This racemization was significantly inhibited by radical scavengers. L-Alanine was also racemized during the same reaction.
ISSN:0916-8451
1347-6947
DOI:10.1271/bbb.120797