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Related Concept Videos

Amyloid Fibrils03:03

Amyloid Fibrils

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. 
Amyloid deposits were observed as early as 1639 in the liver and the spleen.   In 1854, Rudolph Virchow performed iodine staining, normally used to...
Amyloid Fibrils03:03

Amyloid Fibrils

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. 
Amyloid deposits were observed as early as 1639 in the liver and the spleen.   In 1854, Rudolph Virchow performed iodine staining, normally used to...

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Related Experiment Video

Updated: May 27, 2026

Characterizing Individual Protein Aggregates by Infrared Nanospectroscopy and Atomic Force Microscopy
12:58

Characterizing Individual Protein Aggregates by Infrared Nanospectroscopy and Atomic Force Microscopy

Published on: September 12, 2019

Reverse engineering an amyloid aggregation pathway with dimensional analysis and scaling.

J Bailey1, K J Potter, C B Verchere

  • 1Department of Mathematics and Institute of Applied Mathematics, University of British Columbia, Vancouver, Canada.

Physical Biology
|November 29, 2011
PubMed
Summary
This summary is machine-generated.

Human islet amyloid polypeptide (hIAPP) aggregation involves a complex pathway. Our study reveals initiation requires four monomers, followed by pair addition and elongation, crucial for understanding pancreatic beta-cell death.

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Purification and Aggregation of the Amyloid Precursor Protein Intracellular Domain
10:08

Purification and Aggregation of the Amyloid Precursor Protein Intracellular Domain

Published on: August 28, 2012

Related Experiment Videos

Last Updated: May 27, 2026

Characterizing Individual Protein Aggregates by Infrared Nanospectroscopy and Atomic Force Microscopy
12:58

Characterizing Individual Protein Aggregates by Infrared Nanospectroscopy and Atomic Force Microscopy

Published on: September 12, 2019

Purification and Aggregation of the Amyloid Precursor Protein Intracellular Domain
10:08

Purification and Aggregation of the Amyloid Precursor Protein Intracellular Domain

Published on: August 28, 2012

Area of Science:

  • Biochemistry
  • Molecular Biology
  • Cell Biology

Background:

  • Human islet amyloid polypeptide (hIAPP) is a cytotoxic protein implicated in pancreatic beta-cell death.
  • hIAPP aggregation into oligomers and fibrils is a key pathological mechanism.

Purpose of the Study:

  • To elucidate the in vitro aggregation pathway of hIAPP.
  • To identify the critical steps and kinetics governing hIAPP aggregation.
  • To predict the impact of interventions on cytotoxic oligomer formation.

Main Methods:

  • In vitro aggregation assay monitored by thioflavin-T fluorescence.
  • Mass-action kinetics modeling.
  • Scaling analysis to reconstruct the aggregation pathway.

Main Results:

  • hIAPP aggregation initiation requires a nucleus of four monomers.
  • Monomers add in pairs to the nucleus until a stable size of approximately 20 monomers is reached.
  • Fibril elongation occurs via successive addition of single monomers.
  • A secondary fibril-dependent nucleation pathway significantly improves model fit.

Conclusions:

  • The study successfully reverse-engineered the hIAPP aggregation pathway using scaling analysis.
  • Understanding these aggregation dynamics is critical for developing therapeutic strategies against hIAPP-induced cytotoxicity.
  • The findings highlight the potential of modulating nucleation and elongation rates to control toxic oligomer accumulation.