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Screening of DNA aptamer which binds to α-synuclein

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Abstract

α-Synuclein is a native, unfolded protein that causes several neurodegenerative diseases such as dementia with Lewy bodies and Parkinson’s disease. We have now identified the first DNA aptamers against α-synuclein using native PAGE applied to the SELEX method. We call this aptamer “M5-15”; it is the α-synuclein-bound aptamer and was isolated after four cycles of screening. M5-15 is composed of three stem-loop structures that may play an important role in the binding to α-synuclein. Moreover, M5-15 specifically binds to the α-synuclein monomer and oligomer. We expect that this aptamer will become a useful tool in α-synuclein analysis and diagnosis.

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References

  • Ding TT, Lee SJ, Rochet JC, Lansbury PT Jr (2002) Annular alpha-synuclein protofibrils are produced when spherical protofibrils are incubated in solution or bound to brain-derived membranes. Biochemistry 41:10209–10217

    Article  CAS  PubMed  Google Scholar 

  • El-Agnaf OM, Salem SA, Paleologou KE et al (2006) Detection of oligomeric forms of alpha-synuclein protein in human plasma as a potential biomarker for Parkinson’s disease. FASEB J 20:419–425

    Article  CAS  PubMed  Google Scholar 

  • Ellington AD, Szostak JW (1990) In vitro selection of RNA molecules that bind specific ligands. Nature 346:818–822

    Article  CAS  PubMed  Google Scholar 

  • Huang Z, Pei W, Han Y, Jayaseelan S et al (2009) One RNA aptamer sequence, two structures: a collaborating pair that inhibits AMPA receptors. Nucleic Acids Res 37(12):4022–4032

    Article  CAS  PubMed  Google Scholar 

  • Kobayashi M, Kim J, Kobayashi N et al (2006) Pyrroloquinoline quinone (PQQ) prevents fibril formation of alpha-synuclein. Biochem Biophys Res Commun 349:1139–1144

    Article  CAS  PubMed  Google Scholar 

  • Mathews DH, Sabina J, Zuker M et al (1999) Expanded sequence dependence of thermodynamic parameters improves prediction of RNA secondary structure. J Mol Biol 288:911–940

    Article  CAS  PubMed  Google Scholar 

  • Ogasawara D, Hasegawa H, Kaneko K et al (2007) Screening of DNA aptamer against mouse prion protein by competitive selection. Prion 1:248–254

    PubMed  Google Scholar 

  • Paleologou KE, Kragh CL, Mann DM et al (2009) Detection of elevated levels of soluble alpha-synuclein oligomers in post-mortem brain extracts from patients with dementia with Lewy bodies. Brain 132:1093–1101

    Article  PubMed  Google Scholar 

  • Proske D, Gilch S, Wopfner F et al (2002) Prion-protein-specific aptamer reduces PrPSc formation. Chembiochem 3:717–725

    Article  CAS  PubMed  Google Scholar 

  • Rhie A, Kirby L, Sayer N et al (2003) Characterization of 2′-fluoro-RNA aptamers that bind preferentially to disease-associated conformations of prion protein and inhibit conversion. J Biol Chem 278:39697–39705

    Article  CAS  PubMed  Google Scholar 

  • Takahashi T, Tada K, Mihara H (2009) RNA aptamers selected against amyloid beta-peptide (Abeta) inhibit the aggregation of Abeta. Mol Biosyst 5:986–991

    Article  CAS  PubMed  Google Scholar 

  • Tuerk C, Gold L (1990) Systematic evolution of ligands by exponential enrichment: RNA ligands to bacteriophage T4 DNA polymerase. Science 249:505–510

    Article  CAS  PubMed  Google Scholar 

  • Weinreb PH, Zhen W, Poon AW et al (1996) NACP, a protein implicated in Alzheimer’s disease and learning, is natively unfolded. Biochemistry 35(43):13709–13715

    Article  CAS  PubMed  Google Scholar 

  • Weiss S, Proske D, Neumann M et al (1997) RNA aptamers specifically interact with the prion protein PrP. J Virol 71:8790–8797

    CAS  PubMed  Google Scholar 

  • Ylera F, Lurz R, Erdmann VA, Furste JP (2002) Selection of RNA aptamers to the Alzheimer’s disease amyloid peptide. Biochem Biophys Res Commun 290:1583–1588

    Article  CAS  PubMed  Google Scholar 

  • Yoshida W, Sode K, Ikebukuro K (2006) Aptameric enzyme subunit for biosensing based on enzymatic activity measurement. Anal Chem 78:3296–3303

    Article  CAS  PubMed  Google Scholar 

  • Yoshida W, Sode K, Ikebukuro K (2008) Label-free homogeneous detection of immunoglobulin E by an aptameric enzyme subunit. Biotechnol Lett 30(3):421–425

    Article  CAS  PubMed  Google Scholar 

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Correspondence to Kazunori Ikebukuro.

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Tsukakoshi, K., Harada, R., Sode, K. et al. Screening of DNA aptamer which binds to α-synuclein. Biotechnol Lett 32, 643–648 (2010). https://doi.org/10.1007/s10529-010-0200-5

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  • DOI: https://doi.org/10.1007/s10529-010-0200-5

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