Accumulation of collagen molecular unfolding is the mechanism of cyclic fatigue damage and failure in collagenous tissues
© 2020 The Authors. Overuse injuries to dense collagenous tissues are common, but their etiology is poorly understood. The predominant hypothesis that micro-damage accumulation exceeds the rate of biological repair is missing a mechanistic explanation. Here, we used collagen hybridizing peptides to...
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| Format: | Article |
| Language: | English |
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American Association for the Advancement of Science (AAAS)
2021
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| Online Access: | https://hdl.handle.net/1721.1/132713 |
| _version_ | 1826213228283166720 |
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| author | Zitnay, Jared L Jung, Gang Seob Lin, Allen H Qin, Zhao Li, Yang Yu, S Michael Buehler, Markus J Weiss, Jeffrey A |
| author2 | Massachusetts Institute of Technology. Laboratory for Atomistic and Molecular Mechanics |
| author_facet | Massachusetts Institute of Technology. Laboratory for Atomistic and Molecular Mechanics Zitnay, Jared L Jung, Gang Seob Lin, Allen H Qin, Zhao Li, Yang Yu, S Michael Buehler, Markus J Weiss, Jeffrey A |
| author_sort | Zitnay, Jared L |
| collection | MIT |
| description | © 2020 The Authors. Overuse injuries to dense collagenous tissues are common, but their etiology is poorly understood. The predominant hypothesis that micro-damage accumulation exceeds the rate of biological repair is missing a mechanistic explanation. Here, we used collagen hybridizing peptides to measure collagen molecular damage during tendon cyclic fatigue loading and computational simulations to identify potential explanations for our findings. Our results revealed that triple-helical collagen denaturation accumulates with increasing cycles of fatigue loading, and damage is correlated with creep strain independent of the cyclic strain rate. Finite-element simulations demonstrated that biphasic fluid flow is a possible fascicle-level mechanism to explain the rate dependence of the number of cycles and time to failure. Molecular dynamics simulations demonstrated that triple-helical unfolding is rate dependent, revealing rate-dependent mechanisms at multiple length scales in the tissue. The accumulation of collagen molecular denaturation during cyclic loading provides a long-sought "micro-damage"mechanism for the development of overuse injuries. |
| first_indexed | 2024-09-23T15:45:29Z |
| format | Article |
| id | mit-1721.1/132713 |
| institution | Massachusetts Institute of Technology |
| language | English |
| last_indexed | 2024-09-23T15:45:29Z |
| publishDate | 2021 |
| publisher | American Association for the Advancement of Science (AAAS) |
| record_format | dspace |
| spelling | mit-1721.1/1327132024-05-31T20:15:48Z Accumulation of collagen molecular unfolding is the mechanism of cyclic fatigue damage and failure in collagenous tissues Zitnay, Jared L Jung, Gang Seob Lin, Allen H Qin, Zhao Li, Yang Yu, S Michael Buehler, Markus J Weiss, Jeffrey A Massachusetts Institute of Technology. Laboratory for Atomistic and Molecular Mechanics Massachusetts Institute of Technology. Department of Civil and Environmental Engineering © 2020 The Authors. Overuse injuries to dense collagenous tissues are common, but their etiology is poorly understood. The predominant hypothesis that micro-damage accumulation exceeds the rate of biological repair is missing a mechanistic explanation. Here, we used collagen hybridizing peptides to measure collagen molecular damage during tendon cyclic fatigue loading and computational simulations to identify potential explanations for our findings. Our results revealed that triple-helical collagen denaturation accumulates with increasing cycles of fatigue loading, and damage is correlated with creep strain independent of the cyclic strain rate. Finite-element simulations demonstrated that biphasic fluid flow is a possible fascicle-level mechanism to explain the rate dependence of the number of cycles and time to failure. Molecular dynamics simulations demonstrated that triple-helical unfolding is rate dependent, revealing rate-dependent mechanisms at multiple length scales in the tissue. The accumulation of collagen molecular denaturation during cyclic loading provides a long-sought "micro-damage"mechanism for the development of overuse injuries. 2021-10-04T19:27:13Z 2021-10-04T19:27:13Z 2020-08-28 2020-07-14 2021-10-04T18:44:01Z Article http://purl.org/eprint/type/JournalArticle 2375-2548 https://hdl.handle.net/1721.1/132713 Zitnay, Jared L, Jung, Gang Seob, Lin, Allen H, Qin, Zhao, Li, Yang et al. 2020. "Accumulation of collagen molecular unfolding is the mechanism of cyclic fatigue damage and failure in collagenous tissues." Science Advances, 6 (35). en 10.1126/SCIADV.ABA2795 Science Advances Creative Commons Attribution NonCommercial License 4.0 https://creativecommons.org/licenses/by-nc/4.0/ application/pdf American Association for the Advancement of Science (AAAS) Science Advances |
| spellingShingle | Zitnay, Jared L Jung, Gang Seob Lin, Allen H Qin, Zhao Li, Yang Yu, S Michael Buehler, Markus J Weiss, Jeffrey A Accumulation of collagen molecular unfolding is the mechanism of cyclic fatigue damage and failure in collagenous tissues |
| title | Accumulation of collagen molecular unfolding is the mechanism of cyclic fatigue damage and failure in collagenous tissues |
| title_full | Accumulation of collagen molecular unfolding is the mechanism of cyclic fatigue damage and failure in collagenous tissues |
| title_fullStr | Accumulation of collagen molecular unfolding is the mechanism of cyclic fatigue damage and failure in collagenous tissues |
| title_full_unstemmed | Accumulation of collagen molecular unfolding is the mechanism of cyclic fatigue damage and failure in collagenous tissues |
| title_short | Accumulation of collagen molecular unfolding is the mechanism of cyclic fatigue damage and failure in collagenous tissues |
| title_sort | accumulation of collagen molecular unfolding is the mechanism of cyclic fatigue damage and failure in collagenous tissues |
| url | https://hdl.handle.net/1721.1/132713 |
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