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Multidomain Targeting Generates a High‐Affinity Thrombin‐Inhibiting Bivalent Aptamer
Author(s) -
Müller Jens,
Wulffen Bernhard,
Pötzsch Bernd,
Mayer Günter
Publication year - 2007
Publication title -
chembiochem
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.05
H-Index - 126
eISSN - 1439-7633
pISSN - 1439-4227
DOI - 10.1002/cbic.200700535
Subject(s) - aptamer , bivalent (engine) , thrombin , chemistry , computational biology , biophysics , biochemistry , microbiology and biotechnology , biology , platelet , immunology , organic chemistry , metal
More than the sum of its parts . Multidomain targeting aptamers that target human α‐thrombin at two distinct sites simultaneously have been synthesized and functionally characterized. The bivalent aptamer possesses improved activities over those of the individual precursor aptamers of which it is composed. Remarkably, the anticoagulant activity is improved more than 30‐fold; this indicates that the fusion aptamer might represent a novel anticoagulant with immediate clinical relevance.