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

Chem Commun (Camb). 2020 Aug 14;56(63):8940-8943. doi: 10.1039/d0cc02954h. Epub 2020 Jul 8.

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.

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Cattle
  • DEAD-box RNA Helicases / chemistry
  • DEAD-box RNA Helicases / metabolism
  • Fluorescence Polarization
  • G-Quadruplexes*
  • Humans
  • Nucleic Acid Conformation
  • Peptides / chemistry
  • Peptides / metabolism*
  • Promoter Regions, Genetic
  • Protein Binding
  • Proto-Oncogene Proteins c-myc / genetics*

Substances

  • Peptides
  • Proto-Oncogene Proteins c-myc
  • DEAD-box RNA Helicases