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Nucleic Acids Research 2005 33(4):e45; doi:10.1093/nar/gni044
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Published online 3 March 2005

© The Author 2005. Published by Oxford University Press. All rights reserved
The online version of this article has been published under an open access model. Users are entitled to use, reproduce, disseminate, or display the open access version of this article for non-commercial purposes provided that: the original authorship is properly and fully attributed; the Journal and Oxford University Press are attributed as the original place of publication with the correct citation details given; if an article is subsequently reproduced or disseminated not in its entirety but only in part or as a derivative work this must be clearly indicated. For commercial re-use, please contact journals.permissions{at}oupjournals.org

Methods Online

Development of an automated in vitro selection protocol to obtain RNA-based aptamers: identification of a biostable substance P antagonist

Dirk Eulberg, Klaus Buchner, Christian Maasch and Sven Klussmann*

NOXXON Pharma AG Max-Dohrn-Strasse 8-10, 10589 Berlin, Germany

*To whom correspondence should be addressed. Tel: +49 30 726247 240; Fax: +49 30 726247 243; Email: sklussmann{at}noxxon.net

Received August 1, 2004. Revised November 3, 2004. Accepted February 11, 2005.

We have developed an automated SELEX (Systematic Evolution of Ligands by EXponential Enrichment) process that allows the execution of in vitro selection cycles without any direct manual intervention steps. The automated selection protocol is designed to provide for high flexibility and versatility in terms of choice of buffers and reagents as well as stringency of selection conditions. Employing the automated SELEX process, we have identified RNA aptamers to the mirror-image configuration (D-peptide) of substance P. The peptide substance P belongs to the tachykinin family and exerts various biologically important functions, such as peripheral vasodilation, smooth muscle contraction and pain transmission. The aptamer that was identified most frequently was truncated to the 44mer SUP-A-004. The mirror-image configuration of SUP-A-004, the so-called Spiegelmer, has been shown to bind to naturally occurring L-substance P displaying a Kd of 40 nM and to inhibit (IC50 of 45 nM) L-substance P-mediated Ca2+ release in a cell culture assay.


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