Oct 2026· Zenodo (CERN European Organization for Nuclear Research)
Prion Diseases and Protein Misfolding
Abstract
Protein misfolding diseases arise from topological phase transitions in the E8 fiber bundle where non-trivial holonomy around closed loops in configuration space creates wall crossings that trap proteins in pathological configurations. The 240 root vectors define "stability chambers" in fold space, and disease states occur when thermal or oxidative stress shifts the system across these walls, breaking the chord family correspondence established by resonance harmonics. The Ising braid operations predict that amyloid nucleation corresponds to anyon condensation—where the 12 fiber moves collapse into a topologically trivial, energetically favored state. This framework explains the sharp threshold behavior observed in prion propagation and provides a geometric criterion for predicting proteome vulnerability. Author: Andrew Stewart Caldin, Independent Researcher, UK. Part of the E8 Intelligence Research series. Platform: e8intelligence.com
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