TY  - JOUR
A1  - Buff, Maximilian
A1  - Schäfer, Florian
A1  - Wulffen, Bernhard
A1  - Müller, Jens
A1  - Pötzsch, Bernd
A1  - Heckel, Alexander
A1  - Mayer, Günter
T1  - Dependence of aptamer activity on opposed terminal extensions : improvement of light-regulation efficiency
T2  - Nucleic acids research
N2  - 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.
KW  - anticoagulants
KW  - blood coagulation
KW  - thrombin
KW  - coagulation process
Y1  - 2010
UR  - http://publikationen.ub.uni-frankfurt.de/frontdoor/index/index/docId/20247
UR  - https://nbn-resolving.org/urn:nbn:de:hebis:30-85087
SN  - 1362-4962
SN  - 0305-1048
N1  - © The Author(s) 2009. Published by Oxford University Press. This is an Open Access article distributed under the terms of the Creative Commons Attribution Non-Commercial License (http://creativecommons.org/licenses/by-nc/2.5), which permits unrestricted non-commercial use, distribution, and reproduction in any medium, provided the original work is properly cited.
VL  - 38
IS  - 6
SP  - 2111
EP  - 2118
PB  - Oxford Univ. Press
CY  - Oxford
ER  -