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Updated: May 13, 2026
08:53
Characterization of pH-Dependent Reversible Self-Assembly of Amyloid Beta 1-40-Coated Gold Colloids
Published on: March 21, 2025
Computational assembly of polymorphic amyloid fibrils reveals stable aggregates
Mohamed Raef Smaoui1, Frédéric Poitevin, Marc Delarue
1School of Computer Science, McGill University, Montreal, Canada.
Biophysical Journal
|February 28, 2013
Summary
Scientists developed CreateFibril to classify and build complex amyloid fibril structures. This tool predicts fibril stability, validating known structures and revealing new insights into amyloid diseases.
Area of Science:
- Biophysics
- Computational Biology
- Structural Biology
Background:
- Amyloid proteins form polymorphic fibrils implicated in neurodegenerative and cardiac diseases.
- Predicting the stability of large amyloid aggregates remains a challenge.
Purpose of the Study:
- To develop a computational tool for classifying and building complex amyloid fibril structures.
- To assess the stability of these fibrils using a novel computational approach.
Main Methods:
- Developed the CreateFibril software for automated construction of polymorphic amyloid fibrils.
- Employed stability landscapes to analyze fibril structural parameters and stability.
- Utilized a novel dipolar solvent model to assess aqueous stability of large molecular systems.
Main Results:
- Successfully constructed HET-s, Aβ, and amylin fibrils up to 17 nm in length.
- Validated experimental data for HET-s and Aβ fibril structures, predicting key parameters.
- Characterized all known Aβ polymorphic fibrils and elucidated predominant amylin fibrils, suggesting native amylin is more stable than its amyloid form.
Conclusions:
- CreateFibril provides a robust method for modeling and analyzing amyloid fibril structures.
- The study offers novel structural insights into amylin aggregation and stability.
- The findings contribute to understanding amyloid diseases and developing therapeutic strategies.
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