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Issue 8, 2015
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Binding modes of a core-extended metalloporphyrin to human telomeric DNA G-quadruplexes

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Abstract

The molecular recognition of human telomeric G-quadruplexes by a novel cationic π-extended NiII-porphyrin (NiII-TImidP4) is studied in aqueous solutions via (chir)optical spectroscopy, Fluorescence Resonance Energy Transfer (FRET) melting assay, and computational molecular modeling. The results are systematically compared with the recognition by a conventional meso-substituted NiII-porphyrin (NiII-TMPyP4), which allows us to pinpoint the differences in binding modes depending on the G-quadruplex topology. Importantly, FRET melting assays show the higher selectivity of NiII-TImidP4 towards human telomeric G4 than that of NiII-TMPyP4.

Graphical abstract: Binding modes of a core-extended metalloporphyrin to human telomeric DNA G-quadruplexes

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Supplementary files

Article information


Submitted
01 Oct 2014
Accepted
17 Dec 2014
First published
17 Dec 2014

This article is Open Access

Org. Biomol. Chem., 2015,13, 2453-2463
Article type
Paper
Author version available

Binding modes of a core-extended metalloporphyrin to human telomeric DNA G-quadruplexes

J. Rubio-Magnieto, F. Di Meo, M. Lo, C. Delcourt, S. Clément, P. Norman, S. Richeter, M. Linares and M. Surin, Org. Biomol. Chem., 2015, 13, 2453
DOI: 10.1039/C4OB02097A

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