ArticleNucleic acids research2015
Shape-selective recognition of DNA abasic sites by metallohelices: inhibition of human AP endonuclease 1.
Article in Nucleic acids research, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
7 citing papers in PubMed.
- Dicobalt(ii) helices kill colon cancer cellsChemical science · 2024Article
- Metallohelices emulate the properties of short cationic α-helical peptides.Chemical science · 2021Review
- Cavity-Containing [FeFrontiers in chemistry · 2021Article
- Glycoconjugated Metallohelices have Improved Nuclear Delivery and Suppress Tumour Growth In Vivo.Angewandte Chemie (International ed. in English) · 2020Article
- Discovery of selective, antimetastatic and anti-cancer stem cell metallohelicesChemical science · 2019Article
- Antifreeze Protein Mimetic Metallohelices with Potent Ice Recrystallization Inhibition Activity.Journal of the American Chemical Society · 2017Article
- Anticancer metallohelices: nanomolar potency and high selectivity.Chemical science · 2016Article
Corrections and comments
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Authors and funding
3 authors.
Funding
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Abstract
Loss of a base in DNA leading to creation of an abasic (AP) site leaving a deoxyribose residue in the strand, is a frequent lesion that may occur spontaneously or under the action of various physical and chemical agents. Progress in the understanding of the chemistry and enzymology of abasic DNA largely relies upon the study of AP sites in synthetic duplexes. We report here on interactions of diastereomerically pure metallo-helical 'flexicate' complexes, bimetallic triple-stranded ferro-helicates [Fe2(NN-NN)3](4+) incorporating the common NN-NN bis(bidentate) helicand, with short DNA duplexes containing AP sites in different sequence contexts. The results show that the flexicates bind to AP sites in DNA duplexes in a shape-selective manner. They preferentially bind to AP sites flanked by purines on both sides and their binding is enhanced when a pyrimidine is placed in opposite orientation to the lesion. Notably, the Λ-enantiomer binds to all tested AP sites with higher affinity than the Δ-enantiomer. In addition, the binding of the flexicates to AP sites inhibits the activity of human AP endonuclease 1, which is as a valid anticancer drug target. Hence, this finding indicates the potential of utilizing well-defined metallo-helical complexes for cancer chemotherapy.
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