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Thioflavin T acts as a molecular chaperone, accelerating the formation and repair of guanosine-borate hydrogels. This dye enhances hydrogel stiffness and promotes faster assembly of G4 quartets into cross-linked structures.

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Area of Science:

  • Supramolecular Chemistry
  • Materials Science
  • Biophysical Chemistry

Background:

  • Guanosine-lithium borate systems form hydrogels through self-assembly.
  • Molecular chaperones can influence self-assembly processes.
  • Thioflavin T (ThT) is a dye known for binding to amyloid fibrils.

Purpose of the Study:

  • To investigate the role of Thioflavin T (ThT) as a molecular chaperone in the gelation of guanosine and lithium borate.
  • To understand how ThT affects the kinetics, structure, and mechanical properties of the resulting hydrogel.
  • To elucidate the mechanism by which ThT influences hydrogel formation.

Main Methods:

  • Nuclear Magnetic Resonance (NMR) spectroscopy to monitor hydrogelation kinetics.
  • Rheology to measure hydrogel stiffness and repair.
  • Powder X-ray diffraction, UV-Vis, and Circular Dichroism spectroscopy to analyze structure.
  • ThT fluorescence to probe interactions.

Main Results:

  • Substoichiometric concentrations of ThT significantly accelerate hydrogelation.
  • ThT enhances the stiffness and self-repair capabilities of the guanosine-borate hydrogel.
  • Evidence suggests the formation of G-quadruplex (G4) quartets within the Li(+) guanosine-borate system.
  • ThT appears to promote the assembly of G4 quartets into larger structures.

Conclusions:

  • Thioflavin T acts as a molecular chaperone, accelerating the formation of guanosine-borate hydrogels.
  • ThT likely functions by end-stacking on G4 quartets, promoting their assembly into cross-linked hydrogel networks.
  • The study reveals a novel role for ThT in modulating supramolecular assembly and hydrogel properties.