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Towards predictive control of reversible nanoparticle assembly with solid-binding proteins.

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Researchers demonstrate reversible assembly of unmodified nanoparticles using engineered proteins. Controlling pH and protein sequence allows dynamic cluster formation, offering design principles for protein-particle nanocomposites.

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Area of Science:

  • Materials Science
  • Biotechnology
  • Nanotechnology

Background:

  • Stimuli-responsive colloidal systems typically use ligand-functionalized nanoparticles and physico-chemical triggers.
  • Reversible assembly of unmodified nanoparticles with non-covalently bound proteins remains underexplored.

Purpose of the Study:

  • To investigate the reversible assembly and disassembly of unmodified silica nanoparticles mediated by engineered green fluorescent protein.
  • To explore the influence of solution conditions and protein engineering on nanoparticle assembly dynamics.
  • To develop a multiscale model for predicting nanoparticle assembly phenomena.

Main Methods:

  • Engineering green fluorescent protein with silica-binding peptides.
  • Toggling pH between 7.5 and 8.5 to induce assembly/disassembly cycles.
  • Utilizing scattering experiments to capture system behavior.
  • Developing and applying a multiscale model to analyze interparticle forces and predict phenomena.

Main Results:

  • Demonstrated reversible assembly/disassembly of 10-nm silica nanoparticles using engineered green fluorescent protein.
  • Showed that pH, ionic strength, and protein engineering control nanoparticle cluster size (25 nm to micrometer).
  • Identified that high electrolyte environments eliminate reversibility over successive cycles.
  • Validated the multiscale model's accuracy in predicting multi-length scale phenomena.

Conclusions:

  • Solution conditions and protein engineering offer pathways for dynamic control over nanoparticle assembly.
  • The developed model accurately predicts phenomena across multiple length scales.
  • The study provides design principles for creating dynamic protein- and particle-based nanocomposites.