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Nanoscale surface curvature modulates nanoparticle-protein interactions.

Zehui Xia1, Esteban Villarreal2, Hui Wang2

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Summary

Surface curvature of nanoparticles (NPs) impacts protein behavior. Surface-roughened NPs (SRNPs) denature proteins more readily than quasi-spherical NPs (QSNPs), influencing protein conjugation and aggregation.

Keywords:
Bio-nano interfaceBovine serum albuminGold nanoparticlesNanoscale surface curvatureProtein conformationSurface atomic coordination

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Area of Science:

  • Nanotechnology
  • Biophysics
  • Materials Science

Background:

  • Rational design of nanoparticle (NP) surfaces is critical for protein conjugation in various applications.
  • Understanding how NP surface characteristics influence protein behavior is essential for optimizing these applications.

Purpose of the Study:

  • To investigate the effect of local surface curvature of model nanostructures on protein conformation and interfacial behaviors.
  • To compare protein interactions with surface-roughened NPs (SRNPs) and quasi-spherical NPs (QSNPs).

Main Methods:

  • Circular dichroism (CD) spectroscopy to assess protein conformation.
  • Fluorescence emission spectroscopy (FES) to study interfacial behaviors.
  • Isothermal titration calorimetry (ITC) to quantify binding interactions.

Main Results:

  • SRNPs exhibited a higher tendency to denature bovine serum albumin (BSA) and bind more BSA molecules compared to QSNPs.
  • Aggregation of gold NP-BSA complexes was observed and found to be dependent on BSA concentration and NP surface curvature.
  • NP local surface curvature influences protein denaturation and complex aggregation.

Conclusions:

  • Local surface curvature of NPs is a significant factor affecting protein conformation and interfacial behavior.
  • NP surface curvature can be a design strategy to modulate protein denaturation and aggregation, potentially preserving biological function.