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

H nuclear magnetic resonance (NMR) spectroscopy reveals the depletion of soluble species, and oriented fiber X-ray diffraction displays the hallmark cross-β reflections at approximately 4.7 Å and 10 Å. The prolonged formation time implies an activation barrier that is unlikely to require global refolding. Instead, it may reflect early association events such as dimerization or other local rearrangements required for primary nucleation, followed by consolidation into stable intermolecular contacts. Aggregation that preserves a largely native-like fold while establishing cross-β order may reduce recognition by cellular quality-control systems that preferentially target globally unfolded or strongly destabilized states. This provides a plausible framework for how YB-1 derived assemblies could persist under stress and during age-associated proteostasis decline.

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Publication Details

Journal
International Journal of Molecular Sciences
Published
2026-04-16
DOI
https://doi.org/10.3390/ijms27083553
Primary Topic
RNA Research and Splicing
Type
article
Field-Weighted Citation Impact
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article

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

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

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article en

Abstract

H nuclear magnetic resonance (NMR) spectroscopy reveals the depletion of soluble species, and oriented fiber X-ray diffraction displays the hallmark cross-β reflections at approximately 4.7 Å and 10 Å. The prolonged formation time implies an activation barrier that is unlikely to require global refolding. Instead, it may reflect early association events such as dimerization or other local rearrangements required for primary nucleation, followed by consolidation into stable intermolecular contacts. Aggregation that preserves a largely native-like fold while establishing cross-β order may reduce recognition by cellular quality-control systems that preferentially target globally unfolded or strongly destabilized states. This provides a plausible framework for how YB-1 derived assemblies could persist under stress and during age-associated proteostasis decline.

International Journal of Molecular SciencesVol. 27(8)
Mari State University (RU), Institute of Theoretical and Experimental Biophysics (RU), Sirius University of Science and Technology (RU), Gamalei Institute of Epidemiology and Microbiology (RU), Institute of Protein Research (RU), Institute of Cell Biophysics (RU), Keldysh Institute of Applied Mathematics (RU)
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