ArticleBiophysical journal2014
Nanomechanical mapping of hydrated rat tail tendon collagen I fibrils.
Article in Biophysical journal, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.
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Who cites it
20 citing papers in PubMed, 57 citations in OpenAlex.
- Predicting the compression mechanical properties of muscle from microscale indentation mechanics using multiscale mechanical models.Current research in food science · 2026Article
- Atomic Force Microscopy Investigations of Collagen: From Single Molecules to Fibrils.Methods in molecular biology (Clifton, N.J.) · 2026Article
- Quantifying cell traction forces at the single-fiber scale in 3D: An approach based on deformable photopolymerized fiber arrays.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Cold-induced fibrosis and metabolic remodeling in the turtle (Trachemys scripta) ventricle.Acta physiologica (Oxford, England) · 2025Article
- Hybrid cellular Potts and bead-spring modeling of cells in fibrous extracellular matrix.Biophysical journal · 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
- Probing the effect of glycosaminoglycan depletion on integrin interactions with collagen I fibrils in the native extracellular matrix environment.Protein science : a publication of the Protein Society · 2023Article
- Assessment of Efficacy of a Novel Crosslinking Protocol with Intracameral Oxygen (Bubble-CXL) in Increasing the Corneal Stiffness Using Atomic Force Microscopy.Nanomaterials (Basel, Switzerland) · 2022Article
- Self-assembly study of type I collagen extracted from male Wistar Hannover rat tail tendons.Biomaterials research · 2020Article
- Orientation Matters: Polarization Dependent IR Spectroscopy of Collagen from Intact Tendon Down to the Single Fibril Level.Molecules (Basel, Switzerland) · 2020Article
- Stretching Single Collagen Fibrils Reveals Nonlinear Mechanical Behavior.Biophysical journal · 2020Article
- Water-content related alterations in macro and micro scale tendon biomechanics.Scientific reports · 2019Article
- Chronic inflammation deteriorates structure and function of collagen fibril in rat temporomandibular joint disc.International journal of oral science · 2019Article
- The Role of Network Architecture in Collagen Mechanics.Biophysical journal · 2018Article
- Structural characterization of four different naturally occurring porcine collagen membranes suitable for medical applications.PloS one · 2018Article
- Unraveling the role of Calcium ions in the mechanical properties of individual collagen fibrils.Scientific reports · 2017Article
- Internal strain drives spontaneous periodic buckling in collagen and regulates remodeling.Proceedings of the National Academy of Sciences of the United States of America · 2016Article
- Tension tests on mammalian collagen fibrils.Interface focus · 2016Article
- Increased peri-ductal collagen micro-organization may contribute to raised mammographic density.Breast cancer research : BCR · 2016Article
- Bowstring Stretching and Quantitative Imaging of Single Collagen Fibrils via Atomic Force Microscopy.PloS one · 2016Article
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Collagen fibrils play an important role in the human body, providing tensile strength to connective tissues. These fibrils are characterized by a banding pattern with a D-period of 67 nm. The proposed origin of the D-period is the internal staggering of tropocollagen molecules within the fibril, leading to gap and overlap regions and a corresponding periodic density fluctuation. Using an atomic force microscope high-resolution modulus maps of collagen fibril segments, up to 80 μm in length, were acquired at indentation speeds around 10(5) nm/s. The maps revealed a periodic modulation corresponding to the D-period as well as previously undocumented micrometer scale fluctuations. Further analysis revealed a 4/5, gap/overlap, ratio in the measured modulus providing further support for the quarter-staggered model of collagen fibril axial structure. The modulus values obtained at indentation speeds around 10(5) nm/s are significantly larger than those previously reported. Probing the effect of indentation speed over four decades reveals two distinct logarithmic regimes of the measured modulus and point to the existence of a characteristic molecular relaxation time around 0.1 ms. Furthermore, collagen fibrils exposed to temperatures between 50 and 62°C and cooled back to room temperature show a sharp decrease in modulus and a sharp increase in fibril diameter. This is also associated with a disappearance of the D-period and the appearance of twisted subfibrils with a pitch in the micrometer range. Based on all these data and a similar behavior observed for cross-linked polymer networks below the glass transition temperature, we propose that collagen I fibrils may be in a glassy state while hydrated.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.