A short peptide that preferentially binds c-MYC G-quadruplex DNA

G-quadruplexes (G4s) are non-canonical DNA secondary structures. The identification of selective tools to probe individual G4s over the ∼700 000 found in the human genome is key to unravel the biological significance of specific G4s. We took inspiration from a crystal structure of the bovine DHX36 h...

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Veröffentlicht in:Chemical communications (Cambridge, England) England), 2020-08, Vol.56 (63), p.894-8943
Hauptverfasser: Minard, Aisling, Morgan, Danielle, Raguseo, Federica, Di Porzio, Anna, Liano, Denise, Jamieson, Andrew G, Di Antonio, Marco
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Sprache:eng
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Zusammenfassung:G-quadruplexes (G4s) are non-canonical DNA secondary structures. The identification of selective tools to probe individual G4s over the ∼700 000 found in the human genome is key to unravel the biological significance of specific G4s. We took inspiration from a crystal structure of the bovine DHX36 helicase bound to the G4 formed in the promoter region of the oncogene c-MYC to identify a short peptide that preferentially binds MYC G4 with nM affinity over a small panel of parallel and non-parallel G4s tested. G-quadruplexes are nucleic-acids secondary structures that are highly abundant in the human genome. In this work,we identified a short-peptide that displays selectivity for the G-quadruplex formed in the promoter region of the oncogene c-MYC.
ISSN:1359-7345
1364-548X
DOI:10.1039/d0cc02954h