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Coculture Analysis of Extracellular Protein Interactions Affecting Insulin Secretion by Pancreatic Beta Cells
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Insulin aggregation starts at dynamic triple interfaces, originating from solution agitation.

Karim Chouchane1, Thibaut Frachon1, Laurent Marichal1

  • 1Université Grenoble Alpes, CNRS, Grenoble-INP⁎ Institute of Engineering Univ. Grenoble Alpes, LMGP, F-38000 Grenoble, France.

Colloids and Surfaces. B, Biointerfaces
|March 15, 2022
PubMed
Summary

Agitation can cause therapeutic protein instability. This study reveals that dynamic triple interfaces, particularly the triple line, are key drivers of insulin aggregation, even under mild agitation, impacting protein stability.

Keywords:
AgitationInsulinInterfacial adsorptionProtein aggregationProtein dehydrationProtein stabilityTriple interface

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Area of Science:

  • Protein science
  • Biopharmaceutical stability
  • Physical chemistry

Background:

  • Agitation's impact on therapeutic protein stability is critical but not fully understood.
  • The role of dynamic triple interfaces in protein aggregation is under-investigated.

Purpose of the Study:

  • To elucidate the specific contributions of mixing, shear stress, and dynamic triple interfaces to insulin aggregation.
  • To analyze agitation-induced protein aggregation under physiological conditions.

Main Methods:

  • Experimental setups designed to control agitation speed, shear stress, and triple interface extension.
  • Kinetic insulin aggregation studies under intermittent wetting conditions.

Main Results:

  • Strong agitation initiates insulin aggregation; weak agitation sustains aggregate growth.
  • Insulin aggregation rate correlates directly with exposure to dynamic triple interfaces.
  • The triple line (protein solution-air-hydrophobic surface) is identified as a primary site for early aggregation.

Conclusions:

  • Dynamic triple interfaces, especially the triple line, significantly contribute to insulin aggregation during agitation.
  • Understanding these interfacial phenomena is crucial for preventing therapeutic protein aggregation in manufacturing and storage.