ArticleBiophysical journal2011
Contribution of unfolding and intermolecular architecture to fibronectin fiber extensibility.
Article in Biophysical journal, 2011. 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, 19 citations in OpenAlex.
- Fibronectin fiber creep under constant force loading.Acta biomaterialia · 2019Article
- Mechanical Deformation Accelerates Protein Ageing.Angewandte Chemie (International ed. in English) · 2017Article
- Studying early stages of fibronectin fibrillogenesis in living cells by atomic force microscopy.Molecular biology of the cell · 2015Article
- Mechanical forces regulate the interactions of fibronectin and collagen I in extracellular matrix.Nature communications · 2015Article
- Heparin-dependent regulation of fibronectin matrix conformation.Matrix biology : journal of the International Society for Matrix Biology · 2014Article
- Fibronectin conformation regulates the proangiogenic capability of tumor-associated adipogenic stromal cells.Biochimica et biophysica acta · 2013Article
- Using molecular mechanics to predict bulk material properties of fibronectin fibers.PLoS computational biology · 2012Article
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The extracellular matrix contains components with remarkable mechanical properties, including fibronectin (Fn) fibers with extensibilities of >700% strain. We utilized what we consider a novel technique to quantify the extent of molecular unfolding that contributes to Fn fiber extension, and we compared this behavior with stochastic models of Fn fibers with different molecular arrangements. In vitro unfolding as a function of strain was measured by fluorescently labeling cysteines in modules FnIII7 and III15 in artificial Fn fibers. A calibration technique we also consider novel made it possible to demonstrate that 44% of cysteines in these modules were exposed in Fn fibers strained to 421% extension, up from 8% exposure without strain. In silico unfolding was measured by applying a constant strain rate to a fiber represented by a network of wormlike chain springs, each representing an individual Fn molecule. Unfolding rates were calculated with a tension-dependent stochastic model applied to FnIII modules in each molecule. A comparison of these approaches revealed that only a molecular arrangement permitting unequal mechanical loading of Fn molecules recapitulates in vitro unfolding. These data have implications for Fn-dependent mechanotransduction and give insight into how the molecular architecture of natural materials permits such remarkable extensibility.
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Registered trials
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.