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Quantitative mechanistic model for ultrasmall nanoparticle-protein interactions.

Rodrigo S Ferreira1, André L Lira1, Alioscka A Sousa1

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Area of Science:

  • Nanomaterials Science
  • Biophysics
  • Biochemistry

Background:

  • Protein-nanoparticle interactions are crucial for nanomedicine and diagnostics.
  • Understanding the microscopic mechanisms of these interactions remains a challenge.

Purpose of the Study:

  • To investigate the detailed kinetics and molecular mechanisms of ultrasmall gold nanoparticle-protein complexation.
  • To gain insights into the elementary steps and binding affinity changes during complex formation.

Main Methods:

  • Utilized stopped-flow spectroscopy with millisecond time resolution.
  • Investigated binding kinetics between p-mercaptobenzoic acid-coated ultrasmall gold nanoparticles (AuMBA) and fluorescently-labeled ubiquitin.

Main Results:

  • Observed multi-exponential association and dissociation kinetics, indicating a complex, multi-step mechanism.
  • Identified a weakly-bound encounter complex (KD ≈ 9 μM) followed by unimolecular tightening steps.
  • Demonstrated a ~100-fold increase in binding affinity in the final bound state (KD ≈ 0.1 μM).
  • Found that high ionic strength weakens interactions by destabilizing the encounter complex.

Conclusions:

  • Nanoparticle-protein complexation involves distinct steps: initial encounter and subsequent affinity-tightening.
  • The final bound state is weakly stabilized with a lifetime in the seconds range.
  • Electrostatic forces play a significant role in stabilizing the initial encounter complex.