Metal-binding effects of sirtuin inhibitor sirtinol

Sirtinol, a Schiff base derived from 2-hydroxy-1-naphthaldehyde, is an inhibitor of sirtuin proteins, a family of deacetylases active in gene regulation and relevant to the study of cancer growth. The formation of copper(II) and zinc(II) complexes of sirtinol is investigated by spectroscopic and str...

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Bibliographic Details
Published in:Supramolecular chemistry 2016-02, Vol.28 (1-2), p.108-116
Main Authors: Akam, Eman A., Gautam, Ritika, Tomat, Elisa
Format: Article
Language:English
Subjects:
Breast cancer
metal chelators
protein inhibitors
sirtinol
sirtuin proteins
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Summary:Sirtinol, a Schiff base derived from 2-hydroxy-1-naphthaldehyde, is an inhibitor of sirtuin proteins, a family of deacetylases active in gene regulation and relevant to the study of cancer growth. The formation of copper(II) and zinc(II) complexes of sirtinol is investigated by spectroscopic and structural methods. The molecular structure of this protein inhibitor allows for coordination of first-row transition metals in both tridentate and bidentate fashion. In addition, assays in cultured breast cancer cells reveal that Cu II (sirtinol−H) 2 and previously reported Fe III (sirtinol−H)(NO 3 ) 2 present enhanced cytotoxicity when compared to the free ligand, and that the ferric complex causes an increase in intracellular oxidative stress. Transition metal coordination in the biological milieu could therefore contribute additional effects to the biological profile of sirtinol.
ISSN:1061-0278
1029-0478
DOI:10.1080/10610278.2015.1092537