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.
A short peptide that preferentially binds c-MYC G-quadruplex DNA / Minard, Aisling; Morgan, Danielle; Raguseo, Federica; DI PORZIO, Anna; Liano, Denise; Jamieson, Andrew G.; Di Antonio, Marco. - In: CHEMICAL COMMUNICATIONS. - ISSN 1359-7345. - 56:63(2020), pp. 8940-8943. [10.1039/d0cc02954h]
A short peptide that preferentially binds c-MYC G-quadruplex DNA
Anna Di Porzio;
2020
Abstract
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.| File | Dimensione | Formato | |
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