Abstract
Prion disease is caused by conformational change of normal cellular type of prion protein (PrP(c)) folding into abnormal type (PrP(sc)). We succeeded to isolate anti-PrP(c) aptamers. In the presence of competitor RNA, anti-PrP(c) aptamers showed high affinity to PrP(c) (Kd = 10 nM). Heparin has prion binding affinity and partially interfered binding of the aptamer to PrP(c). 2'-Fluoro pyrimidine nucleotide modification still restored their binding affinity (Kd = 20 nM), which was applied for conventional dot- and western-blot assay like as antibody. We also succeeded to isolate anti-PrP(sc) aptamers appearing higher affinity to PrP(sc) in a dose-dependent manner. There is no sequence homology between those anti-PrP(c) and anti-PrP(sc) aptamers.
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