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Unveiling the interaction between DNA G-quadruplexes and RG-rich peptides.
Grasso, Nicola; Graziano, Raffaele; Marzano, Simona; D'Aria, Federica; Merlino, Francesco; Grieco, Paolo; Randazzo, Antonio; Pagano, Bruno; Amato, Jussara.
Afiliación
  • Grasso N; Department of Pharmacy, University of Naples Federico II, 80131 Naples, Italy.
  • Graziano R; Department of Pharmacy, University of Naples Federico II, 80131 Naples, Italy.
  • Marzano S; Department of Pharmacy, University of Naples Federico II, 80131 Naples, Italy.
  • D'Aria F; Department of Pharmacy, University of Naples Federico II, 80131 Naples, Italy.
  • Merlino F; Department of Pharmacy, University of Naples Federico II, 80131 Naples, Italy.
  • Grieco P; Department of Pharmacy, University of Naples Federico II, 80131 Naples, Italy.
  • Randazzo A; Department of Pharmacy, University of Naples Federico II, 80131 Naples, Italy.
  • Pagano B; Department of Pharmacy, University of Naples Federico II, 80131 Naples, Italy. Electronic address: bruno.pagano@unina.it.
  • Amato J; Department of Pharmacy, University of Naples Federico II, 80131 Naples, Italy. Electronic address: jussara.amato@unina.it.
Int J Biol Macromol ; 253(Pt 3): 126749, 2023 Dec 31.
Article en En | MEDLINE | ID: mdl-37689293
ABSTRACT
G-quadruplexes are non-canonical DNA secondary structures formed within guanine-rich strands that play important roles in various biological processes, including gene regulation, telomere maintenance and DNA replication. The biological functions and formation of these DNA structures are strictly controlled by several proteins that bind and stabilize or resolve them. Many G-quadruplex-binding proteins feature an arginine and glycine-rich motif known as the RGG or RG-rich motif. Although this motif plays a crucial role in the recognition of such non-canonical structures, their interaction is still poorly understood. Here, we employed a combination of several biophysical techniques to provide valuable insights into the interaction between a peptide containing an RGG motif shared by numerous human G-quadruplex-binding proteins (NIQI) and various biologically relevant G-quadruplex DNA structures with different topologies. We also shed light on the key amino acids involved in the binding process. Our findings contribute to lay the basis for the development of a new class of peptide-based G-quadruplex ligands as an alternative to small molecules. These ligands may serve as valid tools for interfering in DNA-protein interactions, with potential therapeutic applications.
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Texto completo: 1 Colección: 01-internacional Banco de datos: MEDLINE Asunto principal: G-Cuádruplex Límite: Humans Idioma: En Revista: Int J Biol Macromol Año: 2023 Tipo del documento: Article País de afiliación: Italia

Texto completo: 1 Colección: 01-internacional Banco de datos: MEDLINE Asunto principal: G-Cuádruplex Límite: Humans Idioma: En Revista: Int J Biol Macromol Año: 2023 Tipo del documento: Article País de afiliación: Italia