Multidomain Targeting Generates a High-Affinity Thrombin-Inhibiting Bivalent Aptamer

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 com...

Full description

Saved in:
Bibliographic Details
Published in:Chembiochem : a European journal of chemical biology 2007-12, Vol.8 (18), p.2223-2226
Main Authors: Müller, Jens, Wulffen, Bernhard, Pötzsch, Bernd, Mayer, Günter
Format: Article
Language:English
Subjects:
aptamers
Aptamers, Nucleotide - chemistry
Aptamers, Nucleotide - metabolism
Base Sequence
bivalent ligands
coagulation
Enzyme Inhibitors - chemistry
Ligands
Models, Molecular
Molecular Sequence Data
thrombin
Thrombin - antagonists & inhibitors
Thrombin - metabolism
Citations: Items that this one cites
Items that cite this one
Online Access:Get full text
Tags: Add Tag
No Tags, Be the first to tag this record!
Description
Summary: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.
ISSN:1439-4227
1439-7633
DOI:10.1002/cbic.200700535