ArticleProceedings of the National Academy of Sciences of the United States of America2007
Designing an extracellular matrix protein with enhanced mechanical stability.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2007. 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, 77 citations in OpenAlex.
- Article
- Tension-tuned receptors for synthetic mechanotransduction and intercellular force detection.Nature biotechnology · 2023Article
- Engineering the kinetic stability of a β-trefoil protein by tuning its topological complexity.Frontiers in molecular biosciences · 2023Article
- The role of single protein elasticity in mechanobiology.Nature reviews. Materials · 2023Article
- Contribution of hydrophobic interactions to protein mechanical stability.Computational and structural biotechnology journal · 2022Article
- Mechanism for the Unfolding of the TOP7 Protein in Steered Molecular Dynamics Simulations as Revealed by Mutual Information Analysis.Frontiers in molecular biosciences · 2021Article
- Review
- A novel approach for protein subcellular location prediction using amino acid exposure.BMC bioinformatics · 2013Article
- Promotion of initial cell adhesion on trisuccinimidyl citrate-modified nickel-free high-nitrogen stainless steel.Journal of materials science. Materials in medicine · 2013Article
- The molecular mechanism underlying mechanical anisotropy of the protein GB1.Biophysical journal · 2012Article
- Engineering proteins with enhanced mechanical stability by force-specific sequence motifs.Proteins · 2012Article
- Mechanical anisotropy of ankyrin repeats.Biophysical journal · 2012Article
- Contribution of unfolding and intermolecular architecture to fibronectin fiber extensibility.Biophysical journal · 2011Article
- Enhancing the mechanical stability of proteins through a cocktail approach.Biophysical journal · 2011Article
- Mechanical unfolding of acylphosphatase studied by single-molecule force spectroscopy and MD simulations.Biophysical journal · 2010Article
- Complementary effects of multi-protein components on biomineralization in vitro.Journal of structural biology · 2010Article
- Computational and single-molecule force studies of a macro domain protein reveal a key molecular determinant for mechanical stability.Proceedings of the National Academy of Sciences of the United States of America · 2010Article
- Non-native interactions are critical for mechanical strength in PKD domains.Structure (London, England : 1993) · 2009Article
- Identification of a mechanical rheostat in the hydrophobic core of protein L.Journal of molecular biology · 2009Article
- Single-molecule force spectroscopy distinguishes target binding modes of calmodulin.Proceedings of the National Academy of Sciences of the United States of America · 2009Article
Corrections and comments
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Authors and funding
8 authors at 4 institutions in 2 countries.
Funding
Abstract
The extracellular matrix proteins tenascin and fibronectin experience significant mechanical forces in vivo. Both contain a number of tandem repeating homologous fibronectin type III (fnIII) domains, and atomic force microscopy experiments have demonstrated that the mechanical strength of these domains can vary significantly. Previous work has shown that mutations in the core of an fnIII domain from human tenascin (TNfn3) reduce the unfolding force of that domain significantly: The composition of the core is apparently crucial to the mechanical stability of these proteins. Based on these results, we have used rational redesign to increase the mechanical stability of the 10th fnIII domain of human fibronectin, FNfn10, which is directly involved in integrin binding. The hydrophobic core of FNfn10 was replaced with that of the homologous, mechanically stronger TNfn3 domain. Despite the extensive substitution, FNoTNc retains both the three-dimensional structure and the cell adhesion activity of FNfn10. Atomic force microscopy experiments reveal that the unfolding forces of the engineered protein FNoTNc increase by approximately 20% to match those of TNfn3. Thus, we have specifically designed a protein with increased mechanical stability. Our results demonstrate that core engineering can be used to change the mechanical strength of proteins while retaining functional surface interactions.
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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.