Cookies on this website
We use cookies to ensure that we give you the best experience on our website. If you click 'Continue' we'll assume that you are happy to receive all cookies and you won't see this message again. Click 'Find out more' for information on how to change your cookie settings.

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

DOI

10.1103/PhysRevE.80.041906

Type

Journal article

Journal

Phys Rev E Stat Nonlin Soft Matter Phys

Publication Date

10/2009

Volume

80

Keywords

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