Isolation of Streptomyces sp. KK565 as a Producer of ${\beta}-Amyloid$ Aggregation Inhibitor

  • Hwang, Sung-Eun (Department of Bioscience and Biotechnology, Sejong University) ;
  • Im, Hyung-Min (Department of Biomedical Sciences, National Institute of Health) ;
  • Kim, Dong-Hoon (Department of Bioscience and Biotechnology, Sejong University) ;
  • Shin, Hyun-Ju (Department of Biomedical Sciences, National Institute of Health) ;
  • Shin, Dong-Hoon (Department of Bioscience and Biotechnology, Sejong University) ;
  • Park, Jeong-Eun (Department of Biomedical Sciences, National Institute of Health) ;
  • Jo, In-Ho (Department of Biomedical Sciences, National Institute of Health) ;
  • Kim, Chang-Jin (Korea Research Institute of Bioscience and Biotechnology) ;
  • Yoo, Jong-Shin (Korea Basic Science Institute) ;
  • Kang, Jong-Min (Department of Applied Chemistry, Institute of Bioscience, Sejong University) ;
  • Lim, Dong-Yeon (Department of Applied Chemistry, Institute of Bioscience, Sejong University) ;
  • Ahn-Jo, Snag-Mee (Department of Biomedical Science and Biomedical Brain Research Center, National Institute of Health) ;
  • Kwon, Ho-Jeong (Department of Bioscience and Biotechnology, Sejong University)
  • Published : 2003.10.01

Abstract

${\beta}-amyloid$ ($A{\beta}$) peptides from the proteolytic processing of ${\beta}-amyloid$ precursor protein (${\beta}-APP$) aggregates in the brain to form senile plaques, and their aggregation plays a key role in pathogenesis of Alzheimer's disease (AD). To isolate an active compound that has an $A{\beta}$ aggregation-inhibitory activity, 2,000 microbial metabolite libraries were screened based on their ability to inhibit $A{\beta}$ aggregation by using both Congo red and thioflavin T assays. As a result, a water-soluble fraction of a soil microorganism, KK565, showed a potent $A{\beta}$ aggregation-inhibitory activity. The strain was identified as Streptomyces species, based on the cultural and morphological characteristics, the presence of diaminopimelic acid in the cell wall, and the sugar patterns for the whole-cell extract. In addition, the purification of active principle resulted in identifying a heat-unstable protein responsible for the $A{\beta}$ aggregation-inhibitory activity.

Keywords

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