Fast interaction dynamics of G-quadruplex and RGG-rich peptides unveiled in zero-mode waveguides.

ABSTRACT: G-quadruplexes (GQs), a non-canonical form of DNA, are receiving a huge interest as target sites for potential applications in antiviral and anticancer drug treatments. The biological functions of GQs can be controlled by specifically binding proteins known as GQs binding proteins. Some of the GQs binding proteins contain an arginine and glycine-rich sequence known as RGG peptide. Despite the important role of RGG, the GQs-RGG interaction remains poorly understood. By single molecule measurements, the interaction dynamics can be determined in principle. However, the RGG-GQs interaction occurs at micromolar concentrations, making conventional single-molecule experiments impossible with a diffraction-limited confocal microscope. Here, we use a 120 nm zero-mode waveguide (ZMW) nanoaperture to

SUBMITTER: Patra S 

PROVIDER: S-EPMC8643622 | biostudies-literature | 2021 Dec

REPOSITORIES: biostudies-literature