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Related Concept Videos

Amyloid Fibrils03:03

Amyloid Fibrils

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Amyloid fibrils are aggregates of misfolded proteins.  Under most circumstances, misfolded proteins are either refolded by chaperone proteins or degraded by the proteasome. However, in the case of a mutation or a disease, these proteins can accumulate to form large clusters and often further assemble to form elongated fibers, called fibrils. 
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Protein and Protein Structure02:15

Protein and Protein Structure

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Proteins are one of the most abundant organic molecules in living systems and have the most diverse range of functions of all macromolecules. Proteins may be structural, regulatory, contractile, or protective. They may serve in transport, storage, or membranes; or they may be toxins or enzymes. Their structures, like their functions, vary greatly. They are all, however, amino acid polymers arranged in a linear sequence.
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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 Secretory Vesicles01:05

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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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Protein Folding01:25

Protein Folding

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Proteins are chains of amino acids linked together by peptide bonds. Upon synthesis, a protein folds into a three-dimensional conformation, critical to its biological function. Interactions between its constituent amino acids guide protein folding, and hence the protein structure is primarily dependent on its amino acid sequence.
Protein Structure Is Critical to Its Biological Function
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Insulin action is mediated through a receptor tyrosine kinase, akin to the IGF-1 receptor. The number of receptors per cell varies significantly, from 40 on erythrocytes to 300,000 on adipocytes and hepatocytes. The insulin receptor consists of linked α/β subunit dimers, forming a heterotetramer glycoprotein with two extracellular α subunits and two β subunits spanning the membrane. The α subunits inhibit the inherent tyrosine kinase activity of the β subunits, but...
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Updated: Jun 21, 2025

Interactions with and Membrane Permeabilization of Brain Mitochondria by Amyloid Fibrils
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Cu(II) Specifically Disassembles Insulin Amyloid Nanostructures via Direct Interaction with Cross-β Fibrils.

Shikha Mittal1, Kailash Prasad Prajapati1, Masihuzzaman Ansari1

  • 1Biophysical and Biomaterials Research Laboratory, School of Life Sciences, Jawaharlal Nehru University, New Delhi 110067, India.

Nano Letters
|July 11, 2024
PubMed
Summary

Copper(II) ions effectively break down insulin amyloid structures and prevent new ones from forming. This research reveals how copper ions combat amyloid formation, offering insights for treating amyloid-related diseases.

Keywords:
Cu(II) ionsCu(II)-histidine complexamyloid nanostructure disassemblyantiaggregation effectessential mineralinsulin fibrillation

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Rapid Generation of Amyloid from Native Proteins In vitro
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Area of Science:

  • Biochemistry
  • Materials Science
  • Neuroscience

Background:

  • Amyloid formation, particularly of insulin, is linked to various diseases.
  • Understanding the mechanisms of amyloid inhibition is crucial for therapeutic development.

Purpose of the Study:

  • To investigate the antiamyloid potential of copper(II) ions against insulin amyloidogenesis.
  • To elucidate the molecular interactions between copper(II) ions and insulin amyloid structures.

Main Methods:

  • Utilized copper(II) ions to treat preformed insulin amyloid nanostructures.
  • Assessed the effect of copper(II) ions on insulin monomer fibrillation under aggregation-prone conditions.
  • Analyzed the structural disruption of amyloid fibrils upon interaction with copper(II) ions.

Main Results:

  • Copper(II) ions efficiently disassembled preformed insulin amyloid nanostructures into soluble species.
  • Copper(II) ions suppressed insulin monomer fibrillation under aggregation-prone conditions.
  • Direct interaction of copper(II) ions with the cross-β structure disrupted interchain and intrachain interactions, including H-bonds and hydrophobic contacts.

Conclusions:

  • Copper(II) ions exhibit significant antiamyloidogenic potential against insulin amyloid formation.
  • The study reveals a molecular mechanism involving disruption of amyloid structure and inhibition of protein self-assembly.
  • Findings suggest potential therapeutic strategies utilizing metal ions for amyloid-linked complications.