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논문 기본 정보
- 자료유형
- 학술저널
- 저자정보
- 저널정보
- 한국미생물생명공학회 Journal of Microbiology and Biotechnology Journal of Microbiology and Biotechnology 제28권 제12호
- 발행연도
- 2018.1
- 수록면
- 2,141 - 2,144 (4page)
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초록· 키워드
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Based on previous studies reporting the anti-prion activity of poly-L-lysine and poly-Larginine, 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 PrPSc 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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참고문헌 (19)
참고문헌 신청
Prusiner SB / 1998 / Prions / Proc. Natl. Acad. Sci. USA 95:13363~13383
Prusiner SB / 1983 / Scrapie prions aggregate to form amyloid-like birefringent rods / Cell 35:349~358
Aguzzi A / 2018 / Toward therapy of human prion diseases / Annu. Rev. Pharmacol. Toxicol 58:331~351
Solassol J / 2004 / Cationic phosphorus-containing dendrimers reduce prion replication both in cell culture and in mice infected with scrapie / J. Gen. Virol 85:1791~1799
Cordes H / 2007 / Guanidino- and urea-modified dendrimers as potent solubilizers of misfolded prion protein aggregates under non-cytotoxic conditions: dependence on dendrimer generation and surface charge / Biomacromolecules 8:3578~3583
Prusiner SB / 1983 / Scrapie prions aggregate to form amyloid-like birefringent rods / Cell 35:349~358
Aguzzi A / 2018 / Toward therapy of human prion diseases / Annu. Rev. Pharmacol. Toxicol 58:331~351
Solassol J / 2004 / Cationic phosphorus-containing dendrimers reduce prion replication both in cell culture and in mice infected with scrapie / J. Gen. Virol 85:1791~1799
Cordes H / 2007 / Guanidino- and urea-modified dendrimers as potent solubilizers of misfolded prion protein aggregates under non-cytotoxic conditions: dependence on dendrimer generation and surface charge / Biomacromolecules 8:3578~3583
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