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Single-Molecule Multivalent Interactions Revealed by Plasmon-Enhanced Fluorescence.

Kasper R Okholm1,2, Sjoerd W Nooteboom3, Johan Nygaard Vinther1,4

  • 1Interdisciplinary Nanoscience Center, Aarhus University, Gustav Wieds Vej 14, Aarhus C 8000, Denmark.

ACS Nano
|December 17, 2024
PubMed
Summary
This summary is machine-generated.

Multivalent interactions, crucial in nature and drug design, were studied using plasmon-enhanced fluorescence. This method revealed how DNA ligand flexibility and receptor density influence binding strength and selectivity at the single-molecule level.

Keywords:
DNA nanotechnologyfluorescence enhancementmultivalencyplasmonic nanoparticlessingle-molecule fluorescence

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Area of Science:

  • Biophysics
  • Nanotechnology
  • Molecular Biology

Background:

  • Multivalency enhances binding specificity and strength through multiple weak interactions, mimicking natural processes like immune recognition.
  • Understanding multivalent interactions is key for designing effective drugs and targeted therapies.
  • Single-molecule analysis provides detailed insights into complex binding dynamics.

Purpose of the Study:

  • To develop a method for real-time, single-molecule analysis of multivalent binding kinetics and dynamics.
  • To investigate the impact of DNA ligand length, flexibility, and receptor density on binding characteristics.
  • To introduce a step-binding model incorporating binding restriction for structured macromolecules.

Main Methods:

  • Utilizing plasmon-enhanced fluorescence from nanoparticles for high-sensitivity detection.
  • Employing a DNA Holliday Junction as a model system with tunable valency.
  • Developing a step-binding model with a binding restriction term (ω) to analyze kinetics.

Main Results:

  • Binding strength decreased with increasing spacer length in DNA ligands.
  • Increasing spacer length in trivalent systems activated binding, offering design insights.
  • Receptor density significantly influenced binding strength, demonstrating super selectivity.
  • Plasmon near-field effects allowed observation of binding dynamics during single events.

Conclusions:

  • Plasmon-enhanced fluorescence enables detailed single-molecule studies of multivalent interactions.
  • Ligand design (length, flexibility) and receptor density are critical for controlling binding strength and selectivity.
  • The developed model and methods provide a powerful tool for advancing drug design and understanding biological recognition.