Elongation dynamics of amyloid fibrils: A rugged energy landscape picture

被引：21

作者：

Lee, Chiu Fan ^{[1
]}

Loken, James ^{[2
]}

Jean, Letitia ^{[3
]}

Vaux, David J. ^{[3
]}

机构：

[1] Univ Oxford, Dept Phys, Clarendon Lab, Oxford OX1 3PU, England

[2] Univ Oxford, Dept Phys, Oxford OX1 3RH, England

[3] Univ Oxford, Sir William Dunn Sch Pathol, Oxford OX1 3RE, England

来源：

PHYSICAL REVIEW E | 2009年 / 80卷 / 04期

关键词：

aggregates (materials); biomechanics; diseases; elongation; molecular biophysics; proteins; AGGREGATION-PRONE; IN-SILICO; PREDICTION; PEPTIDES; DIFFUSION; PROTEINS; KINETICS; DISEASE; REGIONS; MODELS;

D O I：

10.1103/PhysRevE.80.041906

中图分类号：

O35 [流体力学]; O53 [等离子体物理学];

学科分类号：

070204 ; 080103 ; 080704 ;

摘要：

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.

引用

页数：6

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