Journal of Microbiology and Biotechnology

The Korean Society for Microbiology and Biotechnology (한국미생물·생명공학회)
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Decrease of Protease-Resistant PrPSc Level in ScN2a Cells by Polyornithine and Polyhistidine

  • Waqas, Muhammad (Department of Pharmacy and Institute of Pharmaceutical Science & Technology, Hanyang University) ;
  • Trinh, Huyen Trang (Department of Pharmacy and Institute of Pharmaceutical Science & Technology, Hanyang University) ;
  • Lee, Sungeun (Department of Pharmacy and Institute of Pharmaceutical Science & Technology, Hanyang University) ;
  • Kim, Dae-hwan (Department of Pharmacy and Institute of Pharmaceutical Science & Technology, Hanyang University) ;
  • Lee, Sang Yeol (Department of Life Science, Gachon University) ;
  • Choe, Kevin K. (Department of Pharmacy and Institute of Pharmaceutical Science & Technology, Hanyang University) ;
  • Ryou, Chongsuk (Department of Pharmacy and Institute of Pharmaceutical Science & Technology, Hanyang University)
  • Received : 2018.07.24
  • Accepted : 2018.10.22
  • Published : 2018.12.28
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Abstract

Based on previous studies reporting the anti-prion activity of poly-${\text\tiny{L}}$-lysine and poly-${\text\tiny{L}}$-arginine, we investigated cationic poly-${\text\tiny{L}}$-ornithine (PLO), poly-${\text\tiny{L}}$-histidine (PLH), anionic poly-${\text\tiny{L}}$-glutamic acid (PLE) and uncharged poly-${\text\tiny{L}}$-threonine (PLT) in cultured cells chronically infected by prions to determine their anti-prion efficacy. While PLE and PLT did not alter the level of $PrP^{Sc}$, PLO and PLH exhibited potent $PrP^{Sc}$ inhibition in ScN2a cells. These results suggest that the anti-prion activity of poly-basic amino acids is correlated with the cationicity of their functional groups. Comparison of anti-prion activity of PLO and PLH proposes that the anti-prion activity of poly-basic amino acids is associated with their acidic cellular compartments.

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