NR AVZP
AU Sekiya,S.; Nishikawa,F.; Noda,K.; Kumar,P.K.; Yokoyama,T.; Nishikawa,S.
TI In vitro selection of RNA aptamers against cellular and abnormal isoform of mouse prion protein
QU Nucleic Acids Symposium Series 2005 Sep; 49: 361-2
IA http://nass.oxfordjournals.org/cgi/reprint/49/1/361
PT journal article
AB Prion disease is caused by conformational change of normal cellular type of prion protein (PrPc) folding into abnormal type (PrPsc). We succeeded to isolate anti-PrPc aptamers. In the presence of competitor RNA, anti-PrPc aptamers showed high affinity to PrPc (Kd = 10 nM). Heparin has prion binding affinity and partially interfered binding of the aptamer to PrPc. 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-PrPsc aptamers appearing higher affinity to PrPsc in a dose-dependent manner. There is no sequence homology between those anti-PrPc and anti-PrPsc aptamers.
MH Animals; Aptamers, Nucleotide/chemistry/*isolation & purification; Mice; PrPc Proteins/*analysis; PrPsc Proteins/*analysis; Protein Isoforms/analysis; SELEX Aptamer Technique
AD Graduate School of Life and Environmental Sciences, University of Tsukuba, Tsukuba, Japan.
SP englisch
PO England