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Protein amyloid fibrils are a form of linear protein aggregates that are implicated in many neurodegenerative diseases. Here, we study the dynamics of amyloid fibril elongation by performing Langevin dynamic simulations on a coarse-grained model of peptides. Our simulation results suggest that the elongation process is dominated by a series of local minimum due to frustration in monomer-fibril interactions. This rugged energy landscape picture indicates that the amount of recycling of monomers at the fibrils' ends before being fibrilized is substantially reduced in comparison to the conventional two-step elongation model. This picture, along with other predictions discussed, can be tested with current experimental techniques.

Original publication




Journal article


Phys Rev E Stat Nonlin Soft Matter Phys

Publication Date





Amyloid, Hydrophobic and Hydrophilic Interactions, Kinetics, Molecular Dynamics Simulation, Protein Multimerization, Protein Structure, Quaternary, Thermodynamics