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Decrease of Protease-Resistant PrP Sc Level in ScN2a Cells by Polyornithine and Polyhistidine

Decrease of Protease-Resistant PrP Sc Level in ScN2a Cells by Polyornithine and Polyhistidine

Muhammad Waqas, Huyen Trinh, Sungeun Lee, Dae-Hwan Kim, Sang Yeol Lee, Kevin K Choe, Chongsuk Ryou

J Microbiol Biotechnol. 2018 Dec 28;28(12):2141-2144.

PMID: 30394046

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 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.

Chemicals Related in the Paper:

Catalog Number	Product Name	Structure	CAS Number	Price
AP82822126	Poly-L-threonine		82822-12-6	Price

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