Morphology and mechanical properties of multi-stranded amyloid fibrils probed by atomistic and coarse-grained simulations
- Authors
- Yoon, Gwonchan; Lee, Myeongsang; Kim, Kyungwoo; Kim, Jae In; Chang, Hyun Joon; Baek, Inchul; Eom, Kilho; Na, Sungsoo
- Issue Date
- 12월-2015
- Publisher
- IOP PUBLISHING LTD
- Keywords
- amyloid proteins; multi-strandness; normal mode analysis; molecular dynamics
- Citation
- PHYSICAL BIOLOGY, v.12, no.6
- Indexed
- SCIE
SCOPUS
- Journal Title
- PHYSICAL BIOLOGY
- Volume
- 12
- Number
- 6
- URI
- https://scholar.korea.ac.kr/handle/2021.sw.korea/91814
- DOI
- 10.1088/1478-3975/12/6/066021
- ISSN
- 1478-3967
- Abstract
- Amyloid fibrils are responsible for pathogenesis of various diseases and exhibit the structural feature of an ordered, hierarchical structure such as multi-stranded helical structure. As the multi-strandedness of amyloid fibrils has recently been found to be highly correlated with their toxicity and infectivity, it is necessary to study how the hierarchical (i.e. multi-stranded) structure of amyloid fibril is formed. Moreover, although it has recently been reported that the nanomechanics of amyloid proteins plays a key role on the amyloid-induced pathogenesis, a critical role that the multi-stranded helical structure of the fibrils plays in their nanomechanical properties has not fully characterized. In this work, we characterize the morphology and mechanical properties of multi-stranded amyloid fibrils by using equilibrium molecular dynamics simulation and elastic network model. It is shown that the helical pitch of multi-stranded amyloid fibril is linearly proportional to the number of filaments comprising the amyloid fibril, and that multi-strandedness gives rise to improving the bending rigidity of the fibril. Moreover, we have also studied the morphology and mechanical properties of a single protofilament (filament) in order to understand the effect of cross-beta structure and mutation on the structures and mechanical properties of amyloid fibrils. Our study sheds light on the underlying design principles showing how the multi-stranded amyloid fibril is formed and how the structure of amyloid fibrils governs their nanomechanical properties.
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