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KMID : 0545120180280122141
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Journal of Microbiology and Biotechnology
2018 Volume.28 No. 12 p.2141 ~ p.2144
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Decrease of protease-resistant PrPSc level in ScN2a cells by polyornithine and polyhistidine
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Waqas Muhammad
Trinh Huyen Trang
Lee Sung-Eun
Kim Dae-Hwan
Lee Sang-Yeol
Choe Kevin K.
Ryou Chong-Suk
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Abstract
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Based on previous studies reporting anti-prion activity of poly-L-lysine and poly-L-arginine, cationic poly-L-ornithine (PLO) and poly-L-histidine (PLH), anionic poly-L-glutamic acid (PLE) and uncharged poly-L-threonine (PLT) were investigated in cultured cells chronically infected by prions to determine 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 anti-prion activity of poly-basic amino acids is correlated with cationicity of their functional groups. Comparison of anti-prion activity of PLO and PLH proposes that anti-prion activity of poly-basic amino acids is associated with the acidic cellular compartments.
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KEYWORD
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Prion, polyornithine, polyhistidine, cationic amino acid polymer
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