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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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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 secretory vesicles release insulin to stimulate blood glucose uptake and regulate carbohydrate metabolism. When the blood glucose levels increase, glucose enters the pancreatic β-islet cells through glucose transporters. Once inside, glucose is metabolized through glycolysis, the citric acid cycle, and the electron transport chain, producing ATP. This increase in ATP concentration closes ATP-sensitive potassium channels, leading to depolarization of the membrane and the opening of...
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Modulating Insulin Aggregation with Charge Variable Cholic Acid-Derived Polymers.

Avisek Bera1, Subhasish Sahoo1, Kalyan Goswami2

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This summary is machine-generated.

Cholic acid (CA)-based cationic polymers effectively inhibit insulin aggregation, acting as anti-amyloidogenic agents. Anionic and neutral polymers showed no significant effect on protein fibrillation.

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Area of Science:

  • Polymer Chemistry
  • Biophysical Chemistry
  • Materials Science

Background:

  • Protein aggregation, particularly insulin fibrillation, is linked to various diseases.
  • Developing effective strategies to control protein aggregation is crucial for therapeutic applications.
  • Cholic acid (CA)-based polymeric architectures offer potential for modulating biological processes.

Purpose of the Study:

  • To design and synthesize charge-variable polymers containing cholate side chains.
  • To investigate the effect of these polymers on insulin fibrillation.
  • To elucidate the mechanism by which CA-based polymers modulate insulin aggregation.

Main Methods:

  • Synthesis of anionic, cationic, and neutral copolymers using reversible addition-fragmentation chain transfer (RAFT) polymerization.
  • Biophysical techniques including spectroscopic (tyrosine fluorescence, Nile red fluorescence, circular dichroism) and microscopic analyses.
  • Isothermal titration calorimetry (ITC) to study polymer-protein interactions.

Main Results:

  • The CA-based cationic polymer (CP-10) significantly inhibited insulin fibrillation in a dose-dependent manner.
  • Anionic (AP-10) and neutral (NP-10) copolymers showed negligible effects on insulin aggregation.
  • Hydrophobic and electrostatic polar interactions were identified as key mechanisms for CP-10's inhibitory activity.

Conclusions:

  • CA-based cationic polymers are effective anti-amyloidogenic agents capable of controlling insulin aggregation.
  • The charge and specific interactions (hydrophobic and electrostatic) of the polymer are critical for its anti-aggregation efficacy.
  • This study presents a novel approach using CA-based cationic polymers for protein aggregation modulation.