2018 ; Vol.28-12: 2141~2144
|Author||Muhammad Waqas, Huyen Trang Trinh, Sungeun Lee, Dae-hwan Kim, Sang Yeol Lee, Kevin K Choe, Chongsuk Ryou|
|Place of duty||Department of Pharmacy and Institute of Pharmaceutical Science & Technology, Hanyang University|
|Title||Decrease of protease-resistant PrPSc level in ScN2a cells by polyornithine and polyhistidine|
J. Microbiol. Biotechnol.2018 ;
|Abstract||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.|
|Key_word||Prion, polyornithine, polyhistidine, cationic amino acid polymer|
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