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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. 
Amyloid deposits were observed as early as 1639 in the liver and the spleen.   In 1854, Rudolph Virchow performed iodine staining,...
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Characterizing Individual Protein Aggregates by Infrared Nanospectroscopy and Atomic Force Microscopy
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Amyloid Formation in Nanoliter Droplets.

Da Yeon Cheong1,2, Wonseok Lee3, Insu Park4

  • 1Department of Biotechnology and Bioinformatics, Korea University, Sejong 30019, Korea.

International Journal of Molecular Sciences
|May 28, 2022
PubMed
Summary

This study presents a microfluidic system for observing amyloid fibril formation in nanoliter droplets. Smaller droplets accelerate amyloid nucleation and growth, offering a novel method for amyloid synthesis.

Keywords:
amyloid formationatomic force microscopyfluorescence assaylysozymenanoliter dropletpolymorphism

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Area of Science:

  • Biochemistry
  • Materials Science
  • Chemical Engineering

Background:

  • Amyloid fibril formation is crucial in medicine and pharmacology.
  • Monitoring nucleation and characterization of amyloid fibrils are essential processes.

Purpose of the Study:

  • To observe and characterize lysozyme amyloid fibril nucleation and formation using a microfluidic system.
  • To investigate the effect of droplet volume on amyloid nucleation and growth.
  • To explore novel methods for amyloid fibril synthesis.

Main Methods:

  • Utilized a facile microfluidic system with nanoliter droplets in a T-junction microchannel.
  • Controlled flow rate and movement of monomer-in-oil emulsion droplets.
  • Employed a fluorescence assay to monitor nucleation and growth based on droplet volume.

Main Results:

  • Reduced lag phase for amyloid nucleation and growth observed at lower droplet volumes.
  • Peculiar phenomenon of high amyloid formation at the edge of bullet-shaped droplets noted.
  • Amyloid fibrils synthesized in nanoliter droplets were shorter and thicker than those from bulk solutions.

Conclusions:

  • The microfluidic system provides a facile procedure to observe and characterize amyloid fibril nucleation and growth.
  • Nanoliter droplet volume influences the kinetics of amyloid formation.
  • This method offers an unconventional synthetic route for amyloid fibrils with distinct morphologies.