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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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Fibril-associated Collagen01:11

Fibril-associated Collagen

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Fibril-associated collagens are a type of collagens present in the extracellular matrix with interrupted triple helices or FACIT (Fibril-associated collagens interrupted triple-helices). FACIT help connect and attach the collagen fibrils with each other as well as with other proteins of the extracellular matrix.
For example, the type II collagen fibrils in cartilage have covalently bound type IX fibril-associated collagens at regular intervals. Other types of fibril-associated collagens are...
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Generation of Straight or Branched Actin Filaments01:14

Generation of Straight or Branched Actin Filaments

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The straight or branched structure formation of actin filaments is controlled by nucleating proteins such as the formins and Arp2/3 complex. Formin-mediated assembly results in straight filaments, whereas Arp2/3 protein complex-mediated assembly results in branched actin filaments.
Arp2/3 Complex
Arp2/3 complex is a seven-subunit complex consisting of two proteins similar to actin- Arp2 and Arp3, and five other subunits that help keep Arp2 and Arp3 inactive. When required, the complex is...
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Type IV Collagen of Basal Lamina01:05

Type IV Collagen of Basal Lamina

2.9K
Type IV collagen is a 400 nm long, network-forming collagen that acts as a barrier between the epithelial and endothelial cells. Type IV collagen  forms the backbone of the basement membrane by scaffolding with laminin, entactin, proteoglycans, and fibronectin. Apart from rendering structural support to the basement membrane, it also helps entail signaling potentials necessary for both pathological and physiological functions.
A type IV collagen molecule has six alpha chains which can...
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Mechanism of Filopodia Formation01:39

Mechanism of Filopodia Formation

3.0K
Filopodia are thin, actin-rich cellular protrusions that play an important role in many fundamental cellular functions. They vary in their occurrence, length, and positioning in different cell types, suggesting their diverse roles.
Their main function is to guide migrating cells during normal tissue morphogenesis or cancer metastasis by recognizing and making initial contacts with the extracellular matrix. However, they can also act as stationary cell anchors or help to establish communication...
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Related Experiment Video

Updated: Jan 10, 2026

Generation of Native, Untagged Huntingtin Exon1 Monomer and Fibrils Using a SUMO Fusion Strategy
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Generation of Native, Untagged Huntingtin Exon1 Monomer and Fibrils Using a SUMO Fusion Strategy

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Tau4RD fibril polymorphism is imprinted during early aggregation.

Ellie I James1,2, Mason Saunders1, Kelly K Lee1

  • 1Department of Medicinal Chemistry, University of Washington, Seattle, WA.

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|November 24, 2025
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Summary

Researchers used pulsed hydrogen-deuterium exchange with mass spectrometry to study tau protein aggregation. This method revealed distinct structural differences in tau subpopulations during early aggregation, offering insights into neurodegenerative disease mechanisms.

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In Vitro Assay for Studying the Aggregation of Tau Protein and Drug Screening
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Related Experiment Videos

Last Updated: Jan 10, 2026

Generation of Native, Untagged Huntingtin Exon1 Monomer and Fibrils Using a SUMO Fusion Strategy
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Generation of Native, Untagged Huntingtin Exon1 Monomer and Fibrils Using a SUMO Fusion Strategy

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Characterizing Individual Protein Aggregates by Infrared Nanospectroscopy and Atomic Force Microscopy
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Characterizing Individual Protein Aggregates by Infrared Nanospectroscopy and Atomic Force Microscopy

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Area of Science:

  • Biochemistry
  • Neuroscience
  • Structural Biology

Background:

  • Microtubule-associated protein tau forms fibrillar species in neurodegenerative diseases.
  • Alzheimer's disease (AD) involves tau deposits like paired helical filaments (PHFs) and straight filaments.
  • Understanding tau aggregation intermediates is crucial for neurodegenerative disease research.

Purpose of the Study:

  • To investigate the early structural changes and polymorphism of tau during aggregation.
  • To differentiate between fibril polymorphism imprinted at nucleation versus later conformational conversion.
  • To explore methods for biasing tau aggregation toward less toxic states.

Main Methods:

  • Pulsed hydrogen-deuterium exchange with mass spectrometry (pulsed HDX-MS) was employed.
  • Studied tau aggregation intermediates and structural conversion.
  • Analyzed tau4RD (truncated tau) aggregation induced by polyphosphate and heparin.

Main Results:

  • Pulsed HDX-MS revealed differences in tau4RD subpopulations within seconds of polyphosphate induction.
  • Distinct structural differences were observed between tau subpopulations formed under different induction conditions (polyphosphate vs. heparin).
  • The study provides insights into the timing and mechanisms of amyloid polymorphism formation.

Conclusions:

  • Amyloid polymorphism in tau may arise from structural rearrangements during aggregation, not solely imprinted at nucleation.
  • Pulsed HDX-MS is a powerful tool for studying transient protein aggregation intermediates.
  • This research contributes to understanding the structural basis of tauopathies and potential therapeutic strategies.