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A Bis‐Zn 2+ ‐Pyridyl‐Salen‐Type Complex Conjugated to the ATP Aptamer: An ATPase‐Mimicking Nucleoapzyme
Author(s) -
Biniuri Yonatan,
Shpilt Zohar,
Albada Bauke,
VázquezGonzález Margarita,
Wolff Mariusz,
Hazan Carina,
Golub Eyal,
Gelman Dimitri,
Willner Itamar
Publication year - 2020
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.201900182
Subject(s) - aptamer , catalysis , chemistry , conjugated system , benzoic acid , stereochemistry , substrate (aquarium) , atpase , nucleic acid , combinatorial chemistry , binding site , enzyme , organic chemistry , biochemistry , biology , ecology , genetics , polymer
Catalytic nucleic acids consisting of a bis‐Zn 2+ ‐pyridyl‐salen‐type ([di‐Zn II 3,5 bis(pyridinylimino) benzoic acid]) complex conjugated to the ATP aptamer act as ATPase‐mimicking catalysts (nucleoapzymes). Direct linking of the Zn 2+ complex to the 3′‐ or 5′‐end of the aptamer (nucleoapzymes I and II) or its conjugation to the 3′‐ or 5′‐end of the aptamer through bis‐thymidine spacers (nucleoapzymes III and IV) provided a set of nucleoapzymes exhibiting variable catalytic activities. Whereas the separated bis‐Zn 2+ ‐pyridyl‐salen‐type catalyst and the ATP aptamer do not show any noticeable catalytic activity, the 3′‐catalyst‐modified nucleoapzyme (nucleoapzyme IV) and, specifically, the nucleoapzyme consisting of the catalyst linked to the 3′‐position through the spacer (nucleoapzyme III) reveal enhanced catalytic features in relation to the analogous nucleoapzyme substituted at the 5′‐position ( k cat =4.37 and 6.88 min −1 , respectively). Evaluation of the binding properties of ATP to the different nucleoapzyme and complementary molecular dynamics simulations suggest that the distance separating the active site from the substrate linked to the aptamer binding site controls the catalytic activities of the different nucleoapzymes.