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Prion Fibril Fragmentation and Propagon Number

Interactive 3D model of prion fibril elongation and chaperone-driven fragmentation: watch propagon number rise or crash across simulated cell divisions and see why a prion trait is lost when fragmentation is too rare.

Molecular Biology3DAdvanced60 FPS📱 Mobile-adapted⇄ 2D version

Beyond the textbook picture of one misfolded protein converting one neighbor on contact, real heritable prion propagation lives or dies on a second process: fragmentation. Growing amyloid fibrils are periodically sheared into shorter pieces by cellular chaperones, and every break mints a new growing end — a new "propagon" capable of templating fresh monomer and of being inherited at the next cell division. This simulator renders that population dynamic in 3D: free, natively-folded monomer drifts in a bounding volume, fibrils elongate by capturing it, chaperone-driven fragmentation splits long fibrils into new seeds, and a periodic cell-division event randomly halves the propagon population the way mitotic partitioning does. Tune the elongation and fragmentation rates to find the threshold where the prion trait is stably inherited versus stochastically cured.

⚙ Under the hood

Watch amyloid fibrils elongate by capturing free monomer and get sheared into new seeds by chaperone-driven fragmentation, then see periodic cell division dilute the propagon pool -- revealing the threshold where a heritable prion state persists or is stochastically cured.

prionprotein misfoldingamyloid fibrilyeast prionmolecular biologyfragmentation kinetics

3D · Three.js / WebGL renderer · 60 FPS target · runs fully client-side, no install