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Moving liquid interfaces drive insulin amyloid aggregation, not shear stress alone. This occurs at the dynamic triple contact line during dewetting, forming fluorescent rings around droplets and covering surfaces with amyloid fibers.

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Area of Science:

  • Biophysics
  • Materials Science
  • Protein Chemistry

Background:

  • Therapeutic protein stability is crucial for drug development.
  • Protein interactions with surfaces and interfaces can impact stability.
  • Automated handling and injection increase protein exposure to dynamic interfaces.

Purpose of the Study:

  • To investigate the effect of a moving triple interface on insulin aggregation.
  • To understand the role of dynamic wetting and dewetting processes on protein stability.
  • To elucidate the mechanism of insulin amyloid fiber formation at moving contact lines.

Main Methods:

  • Utilized a microfluidic setup for real-time analysis.
  • Combined thioflavin T fluorescence and reflection interference microscopy.
  • Monitored insulin aggregation and liquid dewetting simultaneously.

Main Results:

  • Insulin aggregation was observed specifically at the moving triple interface.
  • Hydrodynamic shear stress alone did not induce aggregation.
  • Amyloid aggregates formed fluorescent rings around dewetting droplets, expanding to cover the surface.

Conclusions:

  • The moving triple interface, not shear stress, is the primary driver of insulin aggregation.
  • A model for insulin amyloid fiber growth at dynamic triple contact lines was proposed.
  • Protein adsorption at hydrophobic surfaces, coupled with liquid-air interface exposure, facilitates aggregation.