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Related Concept Videos

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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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The polymerization of G-actin monomers into filamentous F-actin is a multi-step process. Once the F-actins are formed, they can bundle together in different arrangements to form higher-order networks and regulate cellular functions. Common examples include the formation of lamellipodia and filopodia at the cell's leading edge by actin reorganization in a migrating cell. The microvilli on the brush border epithelial cells are also formed through the F-actin network.
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Related Experiment Video

Updated: Jul 7, 2025

Characterization of pH-Dependent Reversible Self-Assembly of Amyloid Beta 1-40-Coated Gold Colloids
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Structural evolution of fibril polymorphs during amyloid assembly.

Martin Wilkinson1, Yong Xu1, Dev Thacker1

  • 1Astbury Centre for Structural Molecular Biology, School of Molecular & Cellular Biology, Faculty of Biological Sciences, University of Leeds, Leeds LS2 9JT, UK.

Cell
|December 22, 2023
PubMed
Summary
This summary is machine-generated.

Amyloid fibril structures change over time during assembly. Cryo-electron microscopy revealed distinct structures forming and disappearing during human islet amyloid polypeptide fibrillation, offering new disease insights.

Keywords:
amyloidamyloid polymorphismcryoEMdiabeteskineticsprotein aggregationprotein fibrilsprotein structurestructural biology

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Area of Science:

  • Biochemistry
  • Structural Biology
  • Molecular Biophysics

Background:

  • Cryoelectron microscopy (cryo-EM) has elucidated static amyloid fibril structures, often associated with diseases.
  • These determined structures represent end-points of assembly, leaving the relationship with early-stage fibrils and potential structural polymorphism unknown.
  • Understanding the dynamic nature of fibril formation is crucial for deciphering disease mechanisms.

Purpose of the Study:

  • To investigate the structural diversity of amyloid fibrils during different stages of in vitro fibrillation.
  • To determine if fibril architecture evolves over time during the assembly process.
  • To explore the implications of dynamic fibril formation for disease progression.

Main Methods:

  • Utilized cryoelectron microscopy (cryo-EM) to analyze amyloid fibril structures.
  • Examined fibrils formed at various time points during the in vitro fibrillation of a disease-related variant of human islet amyloid polypeptide (IAPP-S20G).
  • Conducted time-course analysis with wild-type human islet amyloid polypeptide (hIAPP) to assess generalizability.

Main Results:

  • Observed distinct fibril structures corresponding to the lag, growth, and plateau phases of IAPP-S20G fibrillation.
  • Documented the appearance and disappearance of specific fibril forms as the assembly process progressed.
  • Demonstrated that wild-type hIAPP also exhibits time-dependent changes in fibril structures, indicating a general phenomenon.

Conclusions:

  • Amyloid fibril assembly is a dynamic process involving the formation and disappearance of transiently populated structures.
  • Fibril architecture is not static and evolves over time, potentially influencing pathological properties.
  • These findings provide novel insights into amyloid assembly mechanisms and disease progression.