ArticleProtein science : a publication of the Protein Society2012
Three intrinsically unstructured mussel adhesive proteins, mfp-1, mfp-2, and mfp-3: analysis by circular dichroism.
Article in Protein science : a publication of the Protein Society, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.
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Who cites it
24 citing papers in PubMed, 73 citations in OpenAlex.
- Adverse outcome pathways of titanium dioxide nanoparticles and marine heatwaves on byssal performance in mussels.Eco-Environment & Health · 2026Article
- Synergistic Hydrogels Enabled by Dual-Regulatory Mussel Foot Protein for Advancing Wound Healing.Gels (Basel, Switzerland) · 2026Article
- Investigating byssus self-assembly ofMarine life science & technology · 2026Article
- Structure-Activity Relationships, Molecular Mechanisms, and Ecotoxicological Evaluation Underlying Nucleoside-Mediated Antifouling Activity.Biomolecules · 2026Article
- Development and Functional Characterization of Recombinant Mussel Adhesive Protein for Anti-Oxidative and Anti-Aging Therapeutic Applications.International journal of molecular sciences · 2025Article
- Functional Biomaterials Derived from Protein Liquid-Liquid Phase Separation and Liquid-to-Solid Transition.Advanced materials (Deerfield Beach, Fla.) · 2025Review
- Catechol redox maintenance in mussel adhesion.Nature reviews. Chemistry · 2025Review
- Article
- Protein-Based Biological Materials: Molecular Design and Artificial Production.Chemical reviews · 2023Review
- Solution structure of recombinant Pvfp-5β reveals insights into mussel adhesion.Communications biology · 2022Article
- An essential role of disulfide bonds for the hierarchical self-assembly and underwater affinity of CP20-derived peptides.Frontiers in bioengineering and biotechnology · 2022Article
- Modular genetic design of multi-domain functional amyloids: insights into self-assembly and functional properties.Chemical science · 2019Article
- Universal nanothin silk coatings via controlled spidroin self-assembly.Biomaterials science · 2019Article
- Critical factors for the bulk adhesion of engineered elastomeric proteins.Royal Society open science · 2018Article
- Rapid self-assembly of complex biomolecular architectures during mussel byssus biofabrication.Nature communications · 2017Article
- Mussel adhesion - essential footwork.The Journal of experimental biology · 2017Review
- The microscopic network structure of mussel (Mytilus) adhesive plaques.Journal of the Royal Society, Interface · 2015Article
- Mussel adhesion is dictated by time-regulated secretion and molecular conformation of mussel adhesive proteins.Nature communications · 2015Article
- Peptide Length and Dopa Determine Iron-Mediated Cohesion of Mussel Foot Proteins.Advanced functional materials · 2015Article
- Elastin-like polypeptides as models of intrinsically disordered proteins.FEBS letters · 2015Review
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Authors and funding
2 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Mussel foot proteins (mfps) mediate fouling by the byssal holdfast and have been extensively investigated as models for versatile polymer-mediated underwater adhesion and coatings. However, insights into the structural properties of mfps have lagged far behind the nanomechanical advances, owing in part to the inability of these proteins to crystallize as well as their limited solubility. Here, solution secondary structures of mfp-1, mfp-2, and mfp-3, localized in the mussel byssal cuticle, adhesive plaque, and plaque-substratum interface, respectively, were investigated using circular dichroism. All three have significant extended coil solution structure, but two, mfp-1 and mfp-2, appear to have punctuated regions of structure separated by unstructured domains. Apart from its punctuated distribution, the structure in mfp-1 resembles other structural proteins such as collagen and plant cell-wall proteins with prominent polyproline II helical structure. As in collagen, PP II structure of mfp-1 is incrementally disrupted by increasing the temperature and by raising pH. However, no recognizable change in mfp-1's PP II structure was evident with the addition with Ca²⁺ and Fe³⁺. In contrast, mfp-2 exhibits Ca²⁺- and disulfide-stabilized epidermal growth factor-like domains separated by unstructured sequence. Mfp-2 showed calcium-binding ability. Bound calcium in mfp-2 was not removed by chelation at pH 5.5, but it was released upon reduction of disulfide bonds. Mfp-3, in contrast, appears to consist largely of unstructured extended coils.
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