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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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Amyloid Fibrils03:03

Amyloid Fibrils

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Updated: May 5, 2026

A11-positive &#946;-amyloid Oligomer Preparation and Assessment Using Dot Blotting Analysis
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A11-positive β-amyloid Oligomer Preparation and Assessment Using Dot Blotting Analysis

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YB-1 AP-CSD Forms Cross-β Amyloid Fibrils Without Secondary-Structure Conversion In Vitro.

Maria A Timchenko1, Oxana V Galzitskaya1,2,3, Alexander V Chulkov4

  • 1Institute of Theoretical and Experimental Biophysics, Russian Academy of Sciences, Pushchino 142290, Russia.

International Journal of Molecular Sciences
|May 4, 2026
PubMed
Summary
This summary is machine-generated.

The Y-box binding protein 1 (YB-1) fragment (AP-CSD) forms amyloid fibrils slowly, suggesting a nucleation-dependent process. This aggregation mechanism may allow YB-1 assemblies to evade cellular quality control during stress.

Keywords:
ATR-FTIRX-ray fiber diffractionYB-1amyloid fibrilscircular dichroismcold shock domaincross-β structureprotein aggregationsolution NMR

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Structural Biology

Background:

  • Y-box binding protein 1 (YB-1) is crucial for messenger ribonucleoprotein particle (mRNP) metabolism and stress granule formation.
  • YB-1 self-assembly into fibrils is primarily linked to its cold shock domain (CSD).

Purpose of the Study:

  • To investigate the fibrillization process of the YB-1 fragment spanning residues 1-129 (AP-CSD).
  • To elucidate the structural characteristics and kinetics of AP-CSD fibril formation.

Main Methods:

  • Far-UV circular dichroism (CD) spectroscopy
  • Attenuated total reflection Fourier-transform infrared spectroscopy (ATR-FTIR)
  • Proton nuclear magnetic resonance (1H NMR) spectroscopy
  • Oriented fiber X-ray diffraction

Main Results:

  • AP-CSD forms amyloid fibrils under physiological ionic strength (0.12-0.15 M KCl) over 45-50 hours with linear growth.
  • Secondary structure remains largely unchanged during aggregation, as shown by CD and ATR-FTIR.
  • NMR confirms depletion of soluble species, and X-ray diffraction reveals cross-β structure.

Conclusions:

  • The slow fibrillization kinetics suggest an activation barrier involving early association events rather than global refolding.
  • Preservation of native-like fold during cross-β structure formation may enable YB-1 assemblies to evade cellular quality control.
  • This mechanism provides a framework for YB-1 assembly persistence under cellular stress and during aging-related proteostasis decline.