Elongation dynamics of amyloid fibrils: a rugged energy landscape picture.
Phys Rev E Stat Nonlin Soft Matter Phys
; 80(4 Pt 1): 041906, 2009 Oct.
Article
en En
| MEDLINE
| ID: mdl-19905341
ABSTRACT
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.
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Bases de datos:
MEDLINE
Asunto principal:
Termodinámica
/
Amiloide
Tipo de estudio:
Prognostic_studies
Idioma:
En
Revista:
Phys Rev E Stat Nonlin Soft Matter Phys
Asunto de la revista:
BIOFISICA
/
FISIOLOGIA
Año:
2009
Tipo del documento:
Article
País de afiliación:
Reino Unido