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KMID : 0667720000370000398
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Report Natlonal Institute of Health
2000 Volume.37 No. 0 p.398 ~ p.399
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Identification and purification of 30 kDa protein inhibition amyloid peptide fibrillogenesis from bacteria
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조인호/Jo, I.
권호정/강종민/임동렬/안상미/Kwon, H. J./Kang, J. M./Lim ,D. R./Jo, S. A.
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Abstract
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Purpose: This study was aimed to identify candidate compounds which have biological activities of inhibiting the amyloid fibril formation or solubilizing amyloid fibrils. The result obtained from this study could applied for the development of therapeutic agents for Alzheimer´s disease.
Method: Natural products which contain the inhibitory activity against the amyloid fibril formation were screened by using Conco Red assay or Thioflavin assay, and the blocking activity against amyloid peptide-duced was assayed. Active componants secreted from bacterias were neurotoxicity purified using molecular t-off membranes, several chromatographic techniques and electrophoresis.
Result: Among the 2,000 extracts screened, extracts from more than 10 different bacteria significantly inhibited the amyloid fibril formation. Purification of one extract (#565) which had strong aggregation-inhibiting activity showed that active compound was an approximately 30 kDa hydrophilic protein. The sequence of N-termina. was determined and we are currently in middle of cloning the corresponding gene. We also demonstrated that this protein protected neurons against amyloid-induced neurotoxicity.
Conclusion: A Bioactive compound (30 kDa) which showed the inhibitory activity against the amyloid ril fomation was purified from secreted extract obtained from bactieria and the N-terminal amino acid squence was determined. The cloning and the biological properties of this protein are under investigation in order to determine the possibility for the drug development.
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