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A short peptide that preferentially binds c-MYC G-quadruplex DNA.
- Source :
-
Chemical communications (Cambridge, England) [Chem Commun (Camb)] 2020 Aug 14; Vol. 56 (63), pp. 8940-8943. Date of Electronic Publication: 2020 Jul 08. - Publication Year :
- 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.
- Subjects :
- Amino Acid Sequence
Animals
Cattle
DEAD-box RNA Helicases chemistry
DEAD-box RNA Helicases metabolism
Fluorescence Polarization
Humans
Nucleic Acid Conformation
Peptides chemistry
Promoter Regions, Genetic
Protein Binding
G-Quadruplexes
Peptides metabolism
Proto-Oncogene Proteins c-myc genetics
Subjects
Details
- Language :
- English
- ISSN :
- 1364-548X
- Volume :
- 56
- Issue :
- 63
- Database :
- MEDLINE
- Journal :
- Chemical communications (Cambridge, England)
- Publication Type :
- Academic Journal
- Accession number :
- 32638724
- Full Text :
- https://doi.org/10.1039/d0cc02954h