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
- KOREAN SOC MICROBIOLOGY & BIOTECHNOLOGY
- Keywords
- Prion; polyornithine; polyhistidine; cationic amino acid polymer
- Citation
- JOURNAL OF MICROBIOLOGY AND BIOTECHNOLOGY, v.28, no.12, pp.2141 - 2144
- Journal Title
- JOURNAL OF MICROBIOLOGY AND BIOTECHNOLOGY
- Volume
- 28
- Number
- 12
- Start Page
- 2141
- End Page
- 2144
- URI
- https://scholarworks.bwise.kr/gachon/handle/2020.sw.gachon/3029
- 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.
- Files in This Item
- There are no files associated with this item.
- Appears in
Collections - 바이오나노대학 > 생명과학과 > 1. Journal Articles
![qrcode](https://api.qrserver.com/v1/create-qr-code/?size=55x55&data=https://scholarworks.bwise.kr/gachon/handle/2020.sw.gachon/3029)
Items in ScholarWorks are protected by copyright, with all rights reserved, unless otherwise indicated.