ArticleJournal of the Royal Society, Interface2015
Structure-mechanics relationships of collagen fibrils in the osteogenesis imperfecta mouse model.
Article in Journal of the Royal Society, Interface, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.
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Who cites it
27 citing papers in PubMed, 65 citations in OpenAlex.
- Mechanical characterization ofCell biomaterials · 2026Article
- Molecular drivers of osteogenesis imperfecta: a cellular and extracellular collagen disease.Clinical science (London, England : 1979) · 2025Review
- Nanoscale Structural and Functional Impacts of Disease-Associated Collagen Mutations.bioRxiv : the preprint server for biology · 2025Article
- Water and Collagen: A Mystery Yet to Unfold.Biomacromolecules · 2025Review
- Bone Quality and Mineralization and Effects of Treatment in Osteogenesis Imperfecta.Calcified tissue international · 2024Review
- Elucidating the role of water in collagen self-assembly by isotopically modulating collagen hydration.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- In-silico simulation of nanoindentation on bone using a 2D cohesive finite element model.Journal of the mechanical behavior of biomedical materials · 2024Article
- Progressive alteration of murine bladder elasticity in actinic cystitis detected by Brillouin microscopy.Scientific reports · 2024Article
- Electromechanical Coupling in Collagen Measured under Increasing Relative Humidity.Materials (Basel, Switzerland) · 2023Article
- Single collagen fibrils isolated from high stress and low stress tendons show differing susceptibility to enzymatic degradation by the interstitial collagenase matrix metalloproteinase-1 (MMP-1).Matrix biology plus · 2023Article
- Hierarchical Structure and Properties of the Bone at Nano Level.Bioengineering (Basel, Switzerland) · 2022Article
- Bone hydration: How we can evaluate it, what can it tell us, and is it an effective therapeutic target?Bone reports · 2022Article
- Exploring the Mechanical Properties and Performance of Type-I Collagen at Various Length Scales: A Progress Report.Materials (Basel, Switzerland) · 2022Review
- Removal of glycosaminoglycans affects the in situ mechanical behavior of extrafibrillar matrix in bone.Journal of the mechanical behavior of biomedical materials · 2021Article
- Restoration of Osteogenesis by CRISPR/Cas9 Genome Editing of the MutatedJournal of clinical medicine · 2021Article
- Intrafibrillar mineralization deficiency and osteogenesis imperfecta mouse bone fragility.Journal of the mechanical behavior of biomedical materials · 2021Article
- High-Speed Nanomechanical Mapping of the Early Stages of Collagen Growth by Bimodal Force Microscopy.ACS nano · 2021Article
- Comparative Analysis of the Extracellular Matrix Proteome across the Myotendinous Junction.Journal of proteome research · 2020Article
- Molecular underpinnings of integrin binding to collagen-mimetic peptides containing vascular Ehlers-Danlos syndrome-associated substitutions.The Journal of biological chemistry · 2019Article
- Suitability and limitations of mesenchymal stem cells to elucidate human bone illness.World journal of stem cells · 2019Review
Corrections and comments
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Authors and funding
8 authors at 5 institutions in 4 countries.
Funding
Abstract
The collagen molecule, which is the building block of collagen fibrils, is a triple helix of two α1(I) chains and one α2(I) chain. However, in the severe mouse model of osteogenesis imperfecta (OIM), deletion of the COL1A2 gene results in the substitution of the α2(I) chain by one α1(I) chain. As this substitution severely impairs the structure and mechanics of collagen-rich tissues at the tissue and organ level, the main aim of this study was to investigate how the structure and mechanics are altered in OIM collagen fibrils. Comparing results from atomic force microscopy imaging and cantilever-based nanoindentation on collagen fibrils from OIM and wild-type (WT) animals, we found a 33% lower indentation modulus in OIM when air-dried (bound water present) and an almost fivefold higher indentation modulus in OIM collagen fibrils when fully hydrated (bound and unbound water present) in phosphate-buffered saline solution (PBS) compared with WT collagen fibrils. These mechanical changes were accompanied by an impaired swelling upon hydration within PBS. Our experimental and atomistic simulation results show how the structure and mechanics are altered at the individual collagen fibril level as a result of collagen gene mutation in OIM. We envisage that the combination of experimental and modelling approaches could allow mechanical phenotyping at the collagen fibril level of virtually any alteration of collagen structure or chemistry.
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