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Related Concept Videos

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. 
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At room temperature, the chair conformer of cyclohexane undergoes rapid ring flipping between two equivalent chair conformers at a rate of approximately 105 times per second. These two chair conformers are in equilibrium. The rapid ring flipping results in the interconversion of the axial proton to an equatorial proton and an equatorial to the axial proton. Such interconversions are too rapid and cannot be detected on the NMR timescale. Hence, the NMR spectrometer cannot distinguish between the...
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Discrimination of Formation Processes of Amyloid β Fibrils with Distinct Morphologies Using Rheo-NMR Spectroscopy.

Daichi Morimoto1, Erik Walinda2, Soki Shimizu1

  • 1Department of Molecular Engineering, Graduate School of Engineering, Kyoto University, Kyoto-Daigaku Katsura, Nishikyo-ku, Kyoto 615-8510, Japan.

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Abnormal protein fibril structures, known as amyloid-β (Aβ) fibrils, can adopt different shapes linked to neurodegenerative diseases. This study reveals how shear stress influences Aβ fibril formation and morphology using advanced NMR techniques.

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Area of Science:

  • Neuroscience
  • Biochemistry
  • Biophysics

Background:

  • Abnormal protein aggregates, particularly amyloid fibrils, are implicated in neurodegenerative diseases.
  • Fibril polymorphism, where one protein forms distinct fibril structures, is linked to varying disease phenotypes.
  • The mechanisms driving the formation of different fibril morphologies are not well understood.

Purpose of the Study:

  • To investigate the real-time formation and structural differences of amyloid-β (Aβ) fibrils with distinct morphologies at atomic resolution.
  • To elucidate the role of shear flow in modulating Aβ fibril formation and structure.
  • To explore methods for distinguishing between different Aβ fibril types.

Main Methods:

  • Rheo-NMR spectroscopy to monitor Aβ1-40 fibril formation under shear and quiescent conditions.
  • Atomic-resolution analysis of fibril structures and protein conformations.
  • Molecular dynamics simulations to complement experimental findings.
  • 19F NMR spectroscopy using a fluorinated amyloid-binding dye (FSB) to differentiate fibril types.

Main Results:

  • Under quiescent conditions, Aβ1-40 formed thicker fibrils with rigidification in residues E22-A30.
  • Under shear flow, Aβ1-40 formed thinner fibrils with more elongated conformations.
  • Shear flow was shown to impede specific structural transitions, favoring an alternative fibril morphology.
  • The dye FSB could distinguish between the two Aβ fibril morphologies and their formation pathways via 19F NMR.

Conclusions:

  • Shear stress significantly influences the morphology of Aβ1-40 fibrils at an atomic level.
  • Distinct fibril morphologies arise from shear-dependent modulation of structural transitions during fibrillogenesis.
  • A novel framework using specific dyes and NMR techniques can differentiate pathological fibril types relevant to neurodegenerative diseases.