Mechanical Deformation Mechanisms and Properties of Prion Fibrils Probed by Atomistic Simulations
Abstract Prion fibrils, which are a hallmark for neurodegenerative diseases, have recently been found to exhibit the structural diversity that governs disease pathology. Despite our recent finding concerning the role of the disease-specific structure of prion fibrils in determining their elastic pro...
| Main Authors: | , , , , |
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| Format: | Article |
| Language: | English |
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SpringerOpen
2017-03-01
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| Series: | Nanoscale Research Letters |
| Subjects: | |
| Online Access: | http://link.springer.com/article/10.1186/s11671-017-1966-3 |
| _version_ | 1797710469108072448 |
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| author | Bumjoon Choi Taehee Kim Eue Soo Ahn Sang Woo Lee Kilho Eom |
| author_facet | Bumjoon Choi Taehee Kim Eue Soo Ahn Sang Woo Lee Kilho Eom |
| author_sort | Bumjoon Choi |
| collection | DOAJ |
| description | Abstract Prion fibrils, which are a hallmark for neurodegenerative diseases, have recently been found to exhibit the structural diversity that governs disease pathology. Despite our recent finding concerning the role of the disease-specific structure of prion fibrils in determining their elastic properties, the mechanical deformation mechanisms and fracture properties of prion fibrils depending on their structures have not been fully characterized. In this work, we have studied the tensile deformation mechanisms of prion and non-prion amyloid fibrils by using steered molecular dynamics simulations. Our simulation results show that the elastic modulus of prion fibril, which is formed based on left-handed β-helical structure, is larger than that of non-prion fibril constructed based on right-handed β-helix. However, the mechanical toughness of prion fibril is found to be less than that of non-prion fibril, which indicates that infectious prion fibril is more fragile than non-infectious (non-prion) fibril. Our study sheds light on the role of the helical structure of amyloid fibrils, which is related to prion infectivity, in determining their mechanical deformation mechanisms and properties. |
| first_indexed | 2024-03-12T06:51:41Z |
| format | Article |
| id | doaj.art-e516d60f6170438caee8e3391228f03b |
| institution | Directory Open Access Journal |
| issn | 1931-7573 1556-276X |
| language | English |
| last_indexed | 2024-03-12T06:51:41Z |
| publishDate | 2017-03-01 |
| publisher | SpringerOpen |
| record_format | Article |
| series | Nanoscale Research Letters |
| spelling | doaj.art-e516d60f6170438caee8e3391228f03b2023-09-03T00:15:11ZengSpringerOpenNanoscale Research Letters1931-75731556-276X2017-03-011211910.1186/s11671-017-1966-3Mechanical Deformation Mechanisms and Properties of Prion Fibrils Probed by Atomistic SimulationsBumjoon Choi0Taehee Kim1Eue Soo Ahn2Sang Woo Lee3Kilho Eom4Department of Biomedical Engineering, Yonsei UniversityCollege of Sport Science, Sungkyunkwan University (SKKU)College of Sport Science, Sungkyunkwan University (SKKU)Department of Biomedical Engineering, Yonsei UniversityBiomechanics Laboratory, College of Sport Science, Sungkyunkwan University (SKKU)Abstract Prion fibrils, which are a hallmark for neurodegenerative diseases, have recently been found to exhibit the structural diversity that governs disease pathology. Despite our recent finding concerning the role of the disease-specific structure of prion fibrils in determining their elastic properties, the mechanical deformation mechanisms and fracture properties of prion fibrils depending on their structures have not been fully characterized. In this work, we have studied the tensile deformation mechanisms of prion and non-prion amyloid fibrils by using steered molecular dynamics simulations. Our simulation results show that the elastic modulus of prion fibril, which is formed based on left-handed β-helical structure, is larger than that of non-prion fibril constructed based on right-handed β-helix. However, the mechanical toughness of prion fibril is found to be less than that of non-prion fibril, which indicates that infectious prion fibril is more fragile than non-infectious (non-prion) fibril. Our study sheds light on the role of the helical structure of amyloid fibrils, which is related to prion infectivity, in determining their mechanical deformation mechanisms and properties.http://link.springer.com/article/10.1186/s11671-017-1966-3Prion fibrilMechanical deformation mechanismFracture propertyAtomistic simulation |
| spellingShingle | Bumjoon Choi Taehee Kim Eue Soo Ahn Sang Woo Lee Kilho Eom Mechanical Deformation Mechanisms and Properties of Prion Fibrils Probed by Atomistic Simulations Nanoscale Research Letters Prion fibril Mechanical deformation mechanism Fracture property Atomistic simulation |
| title | Mechanical Deformation Mechanisms and Properties of Prion Fibrils Probed by Atomistic Simulations |
| title_full | Mechanical Deformation Mechanisms and Properties of Prion Fibrils Probed by Atomistic Simulations |
| title_fullStr | Mechanical Deformation Mechanisms and Properties of Prion Fibrils Probed by Atomistic Simulations |
| title_full_unstemmed | Mechanical Deformation Mechanisms and Properties of Prion Fibrils Probed by Atomistic Simulations |
| title_short | Mechanical Deformation Mechanisms and Properties of Prion Fibrils Probed by Atomistic Simulations |
| title_sort | mechanical deformation mechanisms and properties of prion fibrils probed by atomistic simulations |
| topic | Prion fibril Mechanical deformation mechanism Fracture property Atomistic simulation |
| url | http://link.springer.com/article/10.1186/s11671-017-1966-3 |
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