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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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Updated: Nov 24, 2025

In Vitro Growth of Mouse Preantral Follicles Under Simulated Microgravity
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Amyloid fibril formation is suppressed in microgravity.

Hiroaki Matsushita1, Aito Isoguchi2, Masamitsu Okada2

  • 1Department of Amyloidosis Research, Faculty of Pharmaceutical Sciences, Nagasaki International University, 2825-7 Huis Ten Bosch Sasebo, Nagasaki, 859-3298, Japan.

Biochemistry and Biophysics Reports
|December 28, 2020
PubMed
Summary

Earth's gravity accelerates protein amyloid fibril formation. Microgravity conditions reduced amyloidogenicity for insulin and amyloid beta 42 (Aβ42), suggesting space living may alter disease protein aggregation.

Keywords:
Amyloid fibrilsAmyloidosisAβ, amyloid βAβ42DMSO, dimethyl sulfoxideFSB, 1-fluoro-2,5-bis[(E)-3-carboxy-4-hydroxystyryl]benzeneInsulinMicrogravityPBS, phosphate-buffered salineTTRTTR, transthyretinTTRwt, wild-type transthyretinThT, thioflavin T

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Area of Science:

  • Biophysics
  • Space Biology
  • Protein Science

Background:

  • Global environmental changes may necessitate future human habitation in space.
  • Microgravity conditions, prevalent in space, lack convection, potentially altering protein amyloidogenicity.
  • The precise impact of gravity on amyloid fibril formation remains largely uncharacterized.

Purpose of the Study:

  • To investigate the effect of microgravity on the amyloid fibril formation of key amyloidogenic proteins: human insulin, amyloid beta 42 (Aβ42), and transthyretin (TTR).
  • To compare amyloidogenicity under simulated microgravity (10⁻³ g) versus standard Earth gravity (1 g).

Main Methods:

  • Proteins (human insulin, Aβ42, TTRwt) were incubated at specific pH and 37°C under both 1 g and microgravity conditions.
  • Amyloid formation was quantified using the thioflavin T (ThT) fluorescence assay.
  • A cell-based 1-fluoro-2,5-bis[(E)-3-carboxy-4-hydroxystyryl]benzene (FSB) assay was employed to assess amyloidogenicity.

Main Results:

  • Human insulin exhibited decreased amyloidogenicity in microgravity compared to 1 g, observed via both ThT and FSB assays.
  • Aβ42 showed no significant difference in ThT fluorescence but reduced staining intensity in the FSB assay under microgravity.
  • Human wild-type TTR (TTRwt) tended to form fewer amyloid fibrils in microgravity across both measurement methods.

Conclusions:

  • Microgravity conditions appear to reduce the amyloid fibril formation of human insulin and Aβ42.
  • Human TTRwt demonstrated a trend towards reduced amyloid fibril formation in microgravity.
  • These findings suggest that Earth's gravity may play an accelerating role in the process of amyloid fibril formation.