ArticleBiophysical journal2020
Stretching Single Collagen Fibrils Reveals Nonlinear Mechanical Behavior.
Article in Biophysical journal, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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Who cites it
7 citing papers in PubMed.
- Introducing non-enzymatic crosslinks into atomistic simulations of collagen fibrils.Bioinformatics (Oxford, England) · 2026Article
- ColBuilder: flexible structure generation of crosslinked collagen fibrils.Bioinformatics (Oxford, England) · 2025Article
- Bone-inspired stress-gaining elastomer enabled by dynamic molecular locking.Science advances · 2024Article
- Mini review on collagens in normal skin and pathological scars: current understanding and future perspective.Frontiers in medicine · 2024Review
- Cyclic Stretching Triggers Cell Orientation and Extracellular Matrix Remodeling in a Periodontal Ligament 3D In Vitro Model.Advanced healthcare materials · 2023Article
- Exploring the Mechanical Properties and Performance of Type-I Collagen at Various Length Scales: A Progress Report.Materials (Basel, Switzerland) · 2022Review
- Regulators of collagen crosslinking in developing and adult tendons.European cells & materials · 2022Review
Corrections and comments
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Authors and funding
2 authors.
Funding
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Abstract
The mechanical properties of collagen fibrils play an important role in cell-matrix interactions and are a manifestation of their molecular structure. Using a, to our knowledge, novel combination of uniaxial, longitudinal straining and radial nanoindentation, we found that type I collagen fibrils show a pronounced nonlinear behavior in the form of strain stiffening at strains from 0 to 15%, followed by strain softening at strains from 15 to 25%. At the molecular scale, this surprising phenomenon can be explained by the combination of unfolding of disordered domains and breaking of native cross-links at different stages of strain. Fibrils cross-linked artificially by glutaraldehyde do not show such a behavior, and nanoindentation allowed us to measure the mechanics of the overlap and gap regions in the D-banding individually. The results could have consequences for our understanding of matrix mechanics and the influence of excessive glycation, which has been linked with age-related diseases such as diabetes. Furthermore, the simplicity of the straining method could be attractive in other areas of biophysics at the nanometer scale because it does not require any bespoke instrumentation and is easy to use.
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