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Staff Publications

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    'Staff publications' is the digital repository of Wageningen University & Research

    'Staff publications' contains references to publications authored by Wageningen University staff from 1976 onward.

    Publications authored by the staff of the Research Institutes are available from 1995 onwards.

    Full text documents are added when available. The database is updated daily and currently holds about 240,000 items, of which 72,000 in open access.

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Record number 552256
Title A Bis-Zn2+-Pyridyl-Salen-Type Complex Conjugated to the ATP Aptamer : An ATPase-Mimicking Nucleoapzyme
Author(s) Biniuri, Yonatan; Shpilt, Zohar; Albada, Bauke; Vázquez-González, Margarita; Wolff, Mariusz; Hazan, Carina; Golub, Eyal; Gelman, Dimitri; Willner, Itamar
Source ChemBioChem (2019). - ISSN 1439-4227 - p. 1 - 7.
Department(s) Organic Chemistry
Publication type Refereed Article in a scientific journal
Publication year 2019
Keyword(s) catalytic DNA - DNAzymes - microscale thermophoresis - molecular dynamics - nucleic acids

Catalytic nucleic acids consisting of a bis-Zn2+-pyridyl-salen-type ([di-ZnII 3,5 bis(pyridinylimino) benzoic acid]) complex conjugated to the ATP aptamer act as ATPase-mimicking catalysts (nucleoapzymes). Direct linking of the Zn2+ 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-Zn2+-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 (kcat=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.

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