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Related Concept Videos

Insulin: Biosynthesis, Chemistry, and Preparation01:25

Insulin: Biosynthesis, Chemistry, and Preparation

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The endoplasmic reticulum (ER) of pancreatic β-cells synthesizes preproinsulin, which consists of a signal peptide, A and B chains, and a C-peptide. Preproinsulin is then cleaved and folded into proinsulin, which translocates to the Golgi apparatus for sorting and packaging into secretory granules. In these granules, enzymatic clipping generates insulin and C-peptide.
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Insulin preparations are categorized by their duration of action into short-acting and long-acting types. Two strategies are used to modify insulin's absorption and pharmacokinetic profile: slowing the absorption post-subcutaneous injection, or altering human insulin's amino acid sequence or protein structure. These changes retain the insulin's ability to bind to the insulin receptor, but alter its behavior in solution or after injection.
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Encapsulated Control: Shaping Insulin Fibrillation through Polymer Confinement.

Anastasiia Murmiliuk1,2, Sergey K Filippov3, Hiroki Iwase4

  • 1Department of Medical Biotechnology and Translational Medicine, Università degli Studi di Milano, Segrate 20054, Italy.

Biomacromolecules
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Summary
This summary is machine-generated.

Encapsulating insulin in polymers alters its pH and temperature sensitivity. Insulin fibrillation pathways differ when encapsulated, influenced by its oligomeric state within the polyelectrolyte complex.

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Area of Science:

  • Biochemistry
  • Polymer Science
  • Materials Science

Background:

  • Understanding insulin's behavior within polymeric carriers is crucial for drug delivery.
  • Elevated temperatures above 40 °C can significantly impact protein stability and conformation.

Purpose of the Study:

  • To investigate insulin's conformational changes when encapsulated in oppositely charged polymeric nanoparticles.
  • To assess the impact of encapsulation on insulin's pH and temperature sensitivity and fibrillation pathways.

Main Methods:

  • Studied insulin in bulk solution and encapsulated within poly(ethylene oxide)-block-poly(N,N,N-trimethylammonioethyl methacrylate) nanoparticles.
  • Analyzed secondary structure, pH sensitivity, temperature-induced unfolding, and fibrillation pathways.

Main Results:

  • Encapsulation preserved insulin's secondary structure but increased pH resistance.
  • Insulin's temperature resistance decreased, with conformational changes starting at 40 °C within the nanoparticle core.
  • Distinct insulin fibrillation pathways were observed for free versus encapsulated forms, linked to oligomeric state (hexamer vs. trimer).

Conclusions:

  • Polymeric encapsulation modifies insulin's stability and response to environmental factors.
  • The polymer environment influences insulin's oligomeric state, affecting its fibrillation behavior.
  • Findings provide insights into designing stable, effective insulin formulations for therapeutic applications.