title: In vitro selection of RNA aptamers against cellular and abnormal isoform of mouse prion protein.
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.
authors.affiliation: Graduate School of Life and Environmental Sciences, University of Tsukuba, Tsukuba, Japan.
authors.forename: Satoru
authors.initials: S
authors.lastname: Sekiya
authors.forename: Fumiko
authors.initials: F
authors.lastname: Nishikawa
authors.forename: Ken
authors.initials: K
authors.lastname: Noda
authors.forename: P K R
authors.initials: PK
authors.lastname: Kumar
authors.forename: Takashi
authors.initials: T
authors.lastname: Yokoyama
authors.forename: Satoshi
authors.initials: S
authors.lastname: Nishikawa
mesh_terms: D000818:Animals; D052157:Aptamers, Nucleotide / Q000737:chemistry / Q000302:isolation & purification*; D051379:Mice; D018621:PrPC Proteins / Q000032:analysis*; D018620:PrPSc Proteins / Q000032:analysis*; D020033:Protein Isoforms / Q000032:analysis; D052156:SELEX Aptamer Technique
chemical_list: D052157:Aptamers, Nucleotide; D018621:PrPC Proteins; D018620:PrPSc Proteins; D020033:Protein Isoforms