Aptamers against prion proteins and prions.

Abstract

Prion diseases are fatal neurodegenerative and infectious disorders of humans and animals, characterized by structural transition of the host-encoded cellular prion protein (PrP(c)) into the aberrantly folded pathologic isoform PrP(Sc). 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 PrP(Sc) 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.

• Authors: Sabine Gilch, Hermann M Schätzl
• Journal: Cellular and molecular life sciences : CMLS (Cell Mol Life Sci) Vol. 66 Issue 15 Pg. 2445-55 (Aug 2009) ISSN: 1420-9071 [Electronic] Switzerland
• PMID: 19396399 (Publication Type: Journal Article, Review)

Chemical References

• Aptamers, Peptide
• PrPC Proteins
• PrPSc Proteins
• Prions

Topics

• Animals
• Aptamers, Peptide (genetics, metabolism)
• Binding Sites
• Humans
• Models, Molecular
• PrPC Proteins (chemistry, genetics, metabolism)
• PrPSc Proteins (chemistry, genetics, metabolism)
• Prion Diseases (diagnosis, physiopathology, prevention & control, therapy)
• Prions (chemistry, genetics, metabolism)
• Protein Binding
• Protein Conformation