ArticleProceedings of the National Academy of Sciences of the United States of America2022
Structural control of fibrin bioactivity by mechanical deformation.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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Who cites it
14 citing papers in PubMed, 31 citations in OpenAlex.
- Spatiotemporal evaluation of antithrombotic performance for biomaterials through monitoring β-sheet conformation changes at the blood interface.Bioactive materials · 2026Article
- SARS-CoV-2 Spike Protein Amyloid Fibrils Impair Fibrin Formation and Fibrinolysis.Biochemistry · 2025Article
- Fatty acid albumin conjugates mechanically weaken and disrupt degradation of fibrin networks.Acta biomaterialia · 2025Article
- Structural Mechanisms of Forced Unfolding of Double-Stranded Fibrin Oligomers.The journal of physical chemistry. B · 2025Article
- Deconstructing fibrin(ogen) structure.Journal of thrombosis and haemostasis : JTH · 2025Review
- Protofibril packing density of individual fibers alters fibrinolysis.Research and practice in thrombosis and haemostasis · 2025Article
- Using Chemistry To Recreate the Complexity of the Extracellular Matrix: Guidelines for Supramolecular Hydrogel-Cell Interactions.Journal of the American Chemical Society · 2024Review
- Collagen organization and structure inBiomedical optics express · 2024Article
- 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
- Collagen organization and structure inbioRxiv : the preprint server for biology · 2024Article
- Clots reveal anomalous elastic behavior of fiber networks.Science advances · 2024Article
- Cardiac tissue engineering: an emerging approach to the treatment of heart failure.Frontiers in bioengineering and biotechnology · 2024Review
- Visualizing molecular deformation in fibrin networks under tensile loadingChemical communications (Cambridge, England) · 2023Article
- An Exploratory Study Using Next-Generation Sequencing to Identify Prothrombotic Variants in Patients with Cerebral Vein Thrombosis.International journal of molecular sciences · 2023Article
Corrections and comments
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Authors and funding
6 authors at 3 institutions in 3 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Fibrin is the fibrous protein network that comprises blood clots; it is uniquely capable of bearing very large tensile strains (up to 200%) due to multiscale force accommodation mechanisms. Fibrin is also a biochemical scaffold for numerous enzymes and blood factors. The biomechanics and biochemistry of fibrin have been independently studied. However, comparatively little is known about how fibrin biomechanics and biochemistry are coupled: how does fibrin deformation influence its biochemistry? In this study, we show that mechanically induced protein structural changes in fibrin affect fibrin biochemistry. We find that tensile deformation of fibrin leads to molecular structural transitions of α-helices to β-sheets, which reduced binding of tissue plasminogen activator (tPA), an enzyme that initiates fibrin lysis. Moreover, binding of tPA and Thioflavin T, a commonly used β-sheet marker, were mutually exclusive, further demonstrating the mechano-chemical control of fibrin biochemistry. Finally, we demonstrate that structural changes in fibrin suppressed the biological activity of platelets on mechanically strained fibrin due to reduced αIIbβ3 integrin binding. Our work shows that mechanical strain regulates fibrin molecular structure and biological activity in an elegant mechano-chemical feedback loop, which possibly extends to other fibrous biopolymers.
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