Decrease of Protease-Resistant PrPSc Level in ScN2a Cells by Polyornithine and Polyhistidine
- Authors
- Waqas, Muhammad; Huyen Trang Trinh; Lee, Sungeun; Kim, Dae-Hwan; Lee, Sang Yeol; Choe, Kevin K.; Ryou, Chongsuk
- Issue Date
- Dec-2018
- Publisher
- 한국미생물·생명공학회
- Keywords
- Prion; polyornithine; polyhistidine; cationic amino acid polymer
- Citation
- Journal of Microbiology and Biotechnology, v.28, no.12, pp.2141 - 2144
- Indexed
- SCIE
SCOPUS
KCI
- Journal Title
- Journal of Microbiology and Biotechnology
- Volume
- 28
- Number
- 12
- Start Page
- 2141
- End Page
- 2144
- URI
- https://scholarworks.bwise.kr/erica/handle/2021.sw.erica/5080
- DOI
- 10.4014/jmb.1807.07045
- ISSN
- 1017-7825
- Abstract
- Based on previous studies reporting the anti-prion activity of poly-L-lysine and poly-L-arginine, we investigated cationic poly-L-ornithine (PLO), poly-L-histidine (PLH), anionic poly-L-glutamic acid (PLE) and uncharged poly-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 PrPSc, 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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