Dependence of aptamer activity on opposed terminal extensions: improvement of light-regulation efficiency

M.C.R. Buff, F. Schäfer, Bernhard Wulffen, Jens Müller, Bernd Pötzsch, A. Heckel, G. Mayer

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65 Citations (Scopus)


Aptamers that can be regulated with light allow precise control of protein activity in space and time and hence of biological function in general. In a previous study, we showed that the activity of the thrombin-binding aptamer HD1 can be turned off by irradiation using a light activatable 'caged' intramolecular antisense-domain. However, the activity of the presented aptamer in its ON state was only mediocre. Here we studied the nature of this loss in activity in detail and found that switching from 5'- to 3'-extensions affords aptamers that are even more potent than the unmodified HD1. In particular we arrived at derivatives that are now more active than the aptamer NU172 that is currently in phase 2 clinical trials as an anticoagulant. As a result, we present light-regulatable aptamers with a superior activity in their ON state and an almost digital ON/OFF behavior upon irradiation.
Original languageEnglish
Pages (from-to)2111-2118
Number of pages7
JournalNucleic Acids Research
Issue number6
Publication statusPublished - Dec 2009


  • aptamers
  • terminal extensions
  • light-regulation efficiency
  • nucleic acids

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