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Biochemistry Research International
Volume 2016, Article ID 9347468, 11 pages
http://dx.doi.org/10.1155/2016/9347468
Research Article

Potential Properties of Plant Sprout Extracts on Amyloid β

1Nutrition Section, Ageing and Nutrition Research, Yms Laboratory, Gifu 503-1306, Japan
2Laboratory on Ageing & Health Management, Graduate School of Nursing & Health, Aichi Prefectural University, Tohgoku, Kamishidami, Moriyama, Nagoya 463-8502, Japan

Received 7 February 2016; Revised 4 April 2016; Accepted 5 May 2016

Academic Editor: Paul W. Doetsch

Copyright © 2016 Mizue Okada and Yoshinori Okada. This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.

Abstract

The aim of this study is to examine the amyloid β (Aβ) inhibition mechanism of plant sprouts’ aqueous extracts (PSAE). In this study, we screened the effects of five plant sprouts’ extracts on Aβ (1–42) structure modification using gel electrophoresis. In PSAE, no band of Aβ monomer was recognized in Japanese butterbur. Similarly, the Aβ monomer band became light in buckwheat, red cabbage, broccoli, and brussels. The neuroprotective effects of PSAE were evaluated by measuring levels of Aβ in mixtures (Aβ  and PSAE) with Aβ ELISA assay. The treatment with PSAE decreased Aβ levels. The results indicated that the levels of red cabbage, Japanese butterbur, and broccoli were 9.6, 28.0, and 44.0%, respectively. The lowest value was observed with buckwheat. Furthermore, we carried out a Congo Red (CR) and Aβ binding experiment of PSAE to confirm the modification mechanism of PSAE. The correlation coefficient for the absorption spectrum peak of CR was found to be bigger than 0.8 () which proved that the Aβ levels could be attributed to the peak of CR. In conclusion, we demonstrated that treatment with PSAE effectively decreases Aβ concentration. Thus, the mechanism that decreased the Aβ levels may be modification by PSAE.