Cellular and Molecular Life Sciences

, Volume 66, Issue 15, pp 2445–2455

Aptamers against prion proteins and prions


DOI: 10.1007/s00018-009-0031-5

Cite this article as:
Gilch, S. & Schätzl, H.M. Cell. Mol. Life Sci. (2009) 66: 2445. doi:10.1007/s00018-009-0031-5


Prion diseases are fatal neurodegenerative and infectious disorders of humans and animals, characterized by structural transition of the host-encoded cellular prion protein (PrPc) into the aberrantly folded pathologic isoform PrPSc. RNA, DNA or peptide aptamers are classes of molecules which can be selected from complex combinatorial libraries for high affinity and specific binding to prion proteins and which might therefore be useful in diagnosis and therapy of prion diseases. Nucleic acid aptamers, which can be chemically synthesized, stabilized and immobilized, appear more suitable for diagnostic purposes, allowing use of PrPSc as selection target. Peptide aptamers facilitate appropriate intracellular expression, targeting and re-routing without losing their binding properties to PrP, a requirement for potential therapeutic gene transfer experiments in vivo. Elucidation of structural properties of peptide aptamers might be used as basis for rational drug design, providing another attractive application of peptide aptamers in the search for effective anti-prion strategies.


Prion Prion protein Aptamer Peptide aptamer Combinatorial library Anti-prion compound 

Copyright information

© Birkhäuser Verlag, Basel/Switzerland 2009

Authors and Affiliations

  1. 1.Institute of VirologyTechnische Universität MünchenMunichGermany

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