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Related Concept Videos

Insulin Formulations: Types and Delivery01:27

Insulin Formulations: Types and Delivery

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.
Short-acting insulins are divided into rapid-acting...
Insulin: Biosynthesis, Chemistry, and Preparation01:25

Insulin: Biosynthesis, Chemistry, and Preparation

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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Injectable Supramolecular Polymer-Nanoparticle Hydrogels for Cell and Drug Delivery Applications
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Published on: February 7, 2021

Structural characterization of insulin NPH formulations.

Mathias Norrman1, Frantisek Hubálek, Gerd Schluckebier

  • 1Diabetes Protein Engineering, Novo Nordisk A/S, Novo Nordisk Park, 2760 Måløv, Denmark.

European Journal of Pharmaceutical Sciences : Official Journal of the European Federation for Pharmaceutical Sciences
|March 7, 2007
PubMed
Summary

Neutral protamine hagedorn (NPH) insulin

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Area of Science:

  • Biochemistry
  • Structural Biology
  • Pharmacology

Background:

  • Neutral protamine hagedorn (NPH) insulin is a crucial therapeutic formulation for diabetes management.
  • Its extended action profile relies on complexing insulin with zinc and protamine.
  • The precise binding mechanism of protamine to insulin remains largely unknown.

Purpose of the Study:

  • To elucidate the binding mode of protamine within the insulin-protamine complex.
  • To investigate protamine-insulin interactions under various crystallographic conditions.

Main Methods:

  • Crystallographic analysis of insulin-protamine complexes under different conditions (urea, shorter peptide, pharmaceutical-like).
  • High-resolution X-ray diffraction data collection (up to 1.5Å and 2.2Å).
  • Analysis of electron density maps to identify protamine location and conformation.

Main Results:

  • Identified potential protamine density near the solvent channel of the insulin hexamer.
  • Observed protamine binding in an ill-defined conformation across all studied systems.
  • Achieved higher resolution data than previously possible, improving structural insights.

Conclusions:

  • Protamine likely binds to insulin near the zinc-containing solvent channel.
  • The binding conformation of protamine is not well-defined.
  • These findings provide structural insights into NPH insulin formulation.