Food Science and Biotechnology

Korean Society of Food Science and Technology (한국식품과학회)
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Plant Phenolics as ${\beta}$-Secretase (BACE1) Inhibitors

  • Jun, Mi-Ra (Division of Applied Biology and Chemistry, College of Agriculture and Life Sciences, Kyungpook National University) ;
  • Lee, Seung-Ho (College of Pharmacy, Yeungnam University) ;
  • Choi, Sun-Ha (Division of Applied Biology and Chemistry, College of Agriculture and Life Sciences, Kyungpook National University) ;
  • Bae, Ki-Hwan (College of Pharmacy, Chungnam National University) ;
  • Seong, Yeon-Hee (College of Veterinary, Chungbuk National University) ;
  • Lee, Kyung-Bok (Department of Biochemistry, College of Medicine, Konyang University) ;
  • Song, Kyung-Sik (Division of Applied Biology and Chemistry, College of Agriculture and Life Sciences, Kyungpook National University)
  • Published : 2006.08.30
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Abstract

Various plant phenolics were assessed for (${\beta}$-secretase (BACE1) inhibitory activity in order to screen for anti-dementia agents. Among 39 phenolics, eight compounds, 1,2,3-trigalloyl glucopyranoside, acetonyl geraniin, euphorscopin, furosine, helioscopinin A, helioscopinin B, jolkinin, and rugosin E exhibited strong inhibition of BACE1 with $IC_{50}$ values of $5.87{\times}10^{-8}-54.93{\times}10^{-6}\;M$. Among them, rugosin E was the most potent ($IC_{50}$ $5.87{\times}10^{-8}\;M$). The active compounds were shown to be non-competitive inhibitors by Dixon plot. All the phenolic BACE1 inhibitors except furosin also suppressed prolyl endopeptidase (PEP) activity. However, these phenolic compounds caused less inhibition of ${\alpha}$-secretase (tumor necrosis factor a converting enzyme; TACE) and no significant inhibition of other serine proteases such as trypsin, chymotrypsin, and elastase was seen, demonstrating that they are relatively specific to both BACE1 and PEP. No significant structure-activity relationships were found.

Keywords

References

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