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While a significant body of investigations have been focused on the processof protein self-assembly, much less is understood about the reverse process ofa filament breaking due to thermal motion into smaller fragments, ordepolymerization of subunits from the filament ends. Indirect evidence foractin and amyloid filament fragmentation has been reported, although thephenomenon has never been directly observed either experimentally or insimulations. Here we report the direct observation of filament depolymerizationand breakup in a minimal, calibrated model of coarse-grained molecularsimulation. We quantify the orders of magnitude by which the depolymerizationrate from the filament ends $k_\mathrm{off}$ is larger than fragmentation rate$k_{-}$ and establish the law $k_\mathrm{off}/k_- = \exp [( \varepsilon_\| -\varepsilon_\bot) / k_\mathrm{B}T ] = \exp [0.5 \varepsilon / k_\mathrm{B}T ]$,which accounts for the topology and energy of bonds holding the filamenttogether. This mechanism and the order-of-magnitude predictions are wellsupported by direct experimental measurements of depolymerization of insulinamyloid filaments.

Kinetics of fragmentation and dissociation of two-strand protein filaments: Coarse-grained simulations and experiments