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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...
Protein Folding01:22

Protein Folding

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Related Experiment Video

Updated: May 30, 2026

Rapid Generation of Amyloid from Native Proteins In vitro
05:48

Rapid Generation of Amyloid from Native Proteins In vitro

Published on: December 5, 2013

Lysozyme: a model protein for amyloid research.

Rajaram Swaminathan1, Vijay Kumar Ravi, Satish Kumar

  • 1Department of Biotechnology, Indian Institute of Technology Guwahati, Guwahati, Assam, India.

Advances in Protein Chemistry and Structural Biology
|August 18, 2011
PubMed
Summary

Lysozyme aggregation under various conditions, including alkaline pH, is reviewed to understand amyloid formation. This research offers insights into treating systemic nonneuropathic amyloidosis.

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Last Updated: May 30, 2026

Rapid Generation of Amyloid from Native Proteins In vitro
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Published on: December 5, 2013

Biochemical Purification and Proteomic Characterization of Amyloid Fibril Cores from the Brain
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Biochemical Purification and Proteomic Characterization of Amyloid Fibril Cores from the Brain

Published on: April 28, 2022

Area of Science:

  • Biochemistry
  • Structural Biology
  • Biophysics

Background:

  • Lysozyme, discovered in 1922, is a well-established model for protein structure and function studies.
  • Extensive structural data and insights into protein folding dynamics are available for lysozyme.
  • Lysozyme serves as a model protein in biotechnology for recombinant protein recovery from inclusion bodies.

Purpose of the Study:

  • To review and compare mechanisms and morphologies of lysozyme aggregation under diverse in vitro conditions.
  • To enhance understanding of amyloidogenesis by analyzing similarities and differences in aggregation pathways.
  • To highlight the alkaline pH-induced fibrillation of hen lysozyme, a condition extensively studied in the authors' lab.

Main Methods:

  • Comparative analysis of lysozyme aggregation induced by acidic pH, ethanol, guanidinium hydrochloride, and alkaline pH.
  • Detailed examination of aggregate morphology and formation mechanisms across different conditions.
  • Focus on the alkaline pH (12.2) method for inducing lysozyme fibrillation.

Main Results:

  • Multiple in vitro conditions effectively induce lysozyme fibrillation, each with distinct mechanisms and aggregate structures.
  • Alkaline pH-induced fibrillation provides a specific model for studying amyloidogenesis.
  • Lysozyme's enzymatic activity allows for quantification of native protein, aiding in the study of aggregation inhibition.

Conclusions:

  • Understanding lysozyme aggregation mechanisms is crucial for developing therapeutic strategies against systemic nonneuropathic amyloidosis.
  • Lysozyme's rich data and amenability to in vitro aggregation/inhibition studies make it an ideal model for amyloidogenesis research.
  • Inhibition studies using antibodies or small molecules, monitored by enzymatic activity, are promising for therapeutic development.