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Amyloid Fibrils03:03

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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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Deciphering Amyloid Fibril Formation through Protein Concentration by Optical Trapping.

Teruki Sugiyama1,2, Shu-Ting Weng1, Tien Chen1

  • 1Department of Applied Chemistry and Center for Emergent Functional Matter Science, National Yang Ming Chiao Tung University, No. 1001, Daxue Rd. East Dist, Hsinchu 300093, Taiwan.

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PubMed
Summary
This summary is machine-generated.

Optical trapping precisely tracks protein dynamics during amyloid formation. Apoferritin condensates form rapidly, with pH influencing concentration and elongation rates, revealing critical factors in amyloid fibril development.

Keywords:
amyloid fibril formationapoferritinoptical trappingpH controlprotein aggregation

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Area of Science:

  • Biophysics
  • Materials Science
  • Biochemistry

Background:

  • Amyloid fibril formation is implicated in various diseases.
  • Understanding the early stages of protein aggregation is crucial for therapeutic development.
  • Apoferritin (Fer8) serves as a model protein for studying amyloidogenesis.

Purpose of the Study:

  • To investigate the real-time dynamics of protein concentration during amyloid fibril formation.
  • To explore the influence of pH (pD) on apoferritin condensation and fibril elongation.
  • To elucidate the role of optical trapping in dissecting early-stage amyloidogenesis.

Main Methods:

  • Utilized optical trapping combined with time-lapse transmission and fluorescence imaging.
  • Observed apoferritin (Fer8) condensation and growth at the laser focus.
  • Analyzed protein concentration dynamics and secondary structure changes at different pH (pD) conditions.

Main Results:

  • Apoferritin condensates formed within 30 min, reaching ~1.2 μm diameter.
  • Initial trapping efficiency varied with pD, being higher at pD 8.4.
  • Acidic conditions (pD 1.5, 2.0) showed a delayed but significant second-phase concentration increase.
  • A critical concentration (0.53-0.63 mM) was identified for rapid ThT fluorescence onset.
  • Optical trapping suggested specific molecular alignment beyond simple concentration effects.

Conclusions:

  • Optical trapping is a powerful tool for real-time observation of protein aggregation dynamics.
  • pH significantly impacts apoferritin condensation, concentration, and amyloid fibril elongation rates.
  • Findings provide insights into the pD-dependent interplay of protein structure, nucleation, and elongation in early amyloid formation.