Isolation of Streptomyces sp. KK565 as a Producer of b-Amyloid Aggregation Inhibitor

β-amyloid$ ($A{\beta}$) peptides from the proteolytic processing of β-amyloid$ precursor protein (β-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 $A{\beta}$ aggr...

Full description

Saved in:
Bibliographic Details
Published inJournal of microbiology and biotechnology pp. 809 - 814
Main Authors HWANG,SUNGEUN, HYUNG-MINIM, DONGHOONKIM, HYUN-JUSHIN, DONGHOONSHIN, JEONGEUNPARK, INHOJO, CHANGJINKIM, JONG-SHINYOO, JONGMINKANG, DONGYEOLLIM, 안상미, HOJEONGKWON
Format Journal Article
LanguageEnglish
Published 한국미생물·생명공학회 01.08.2003
Subjects
Online AccessGet full text

Cover

Loading…
More Information
Summary:β-amyloid$ ($A{\beta}$) peptides from the proteolytic processing of β-amyloid$ precursor protein (β-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. KCI Citation Count: 2
Bibliography:G704-000169.2003.13.5.004
ISSN:1017-7825