Iron-Clad Fibers: A Metal-Based Biological Strategy for Hard Flexible Coatings
Open accessAbstract
The extensible byssal threads of marine mussels are shielded from abrasion in wave-swept habitats by an outer cuticle that is largely proteinaceous and approximately fivefold harder than the thread core. Threads from several species exhibit granular cuticles containing a protein that is rich in the catecholic amino acid 3,4-dihydroxyphenylalanine (dopa) as well as inorganic ions, notably Fe3+. Granular cuticles exhibit a remarkable combination of high hardness and high extensibility. We explored byssus cuticle chemistry by means of in situ resonance Raman spectroscopy and demonstrated that the cuticle is a polymeric scaffold stabilized by catecholato-iron chelate complexes having an unusual clustered distribution. Consistent with byssal cuticle chemistry and mechanics, we present a model in which dense cross-linking in the granules provides hardness, whereas the less cross-linked matrix provides extensibility.
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Coordination bonding and strong chelating bonding with transition metal compounds occur between catechol or diketone groups on the polydopamine coating layer and the interface of inorganic biosubstitutes, along with protein cross-linking.
“Such coordination bonding and strong chelating bonding with transition metal compound occur between catechol or diketone groups on the PDA coating layer and the interface of inorganic biosubstitutes along with the protein cross-linking [61–66].”
From Polydopamine-Assisted Surface Modification for Bone Biosubstitutes (2016) · cites this paper as [62]
The indexed passage labeled Abstract (page unavailable) describes catechol–iron coordination and cross-links between mussel foot protein chains, supporting the general bonding mechanism. It does not establish that such bonds occur at an inorganic biosubstitute interface on a polydopamine (PDA) coating, or that diketone groups participate. (LLM, conf=0.87)
Experimental — accuracy not yet measuredOn certain specific inorganic biosubstitute surfaces, such as negatively charged oxidized silicone, electrostatic interaction from protonated amino groups can enhance adhesion of biomolecules to the surface.
“Meanwhile, on certain specific surfaces of inorganic biosubstitutes (e.g., negatively charged oxidized silicone), the electrostatic interaction from protonated amino group can also enhance the adhesion of biomolecules to the surface of biosubstitutes [62, 67].”
From Polydopamine-Assisted Surface Modification for Bone Biosubstitutes (2016) · cites this paper as [62]
The paper’s discussion of mussel byssus cuticles describes dopa–metal cross-links and their mechanical role (section labeled Abstract; page unavailable). Searches for protonated amino groups, electrostatic surface adhesion, and oxidized silicone found no passage addressing the claimed mechanism. (LLM, conf=0.76)
Experimental — accuracy not yet measured
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Cites
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Mussel-Inspired Adhesives and Coatings
Lee, B. P., Messersmith, P. B., Israelachvili, J. N., & Waite, J. H. (2011) · Annual Review of Materials Research · doi:10.1146/annurev-matsci-062910-100429 · Cited by 1,668 · see citing works
Self-citationBiological materials: Functional adaptations and bioinspired designs
Chen, P.-Y., McKittrick, J., & Meyers, M. A. (2012) · Progress in Materials Science · doi:10.1016/j.pmatsci.2012.03.001 · Cited by 766 · see citing works
Recent progress in synthesis and application of mussel-inspired adhesives
Guo, Q., Chen, J., Wang, J., Zeng, H., & Yu, J. (2020) · Nanoscale · doi:10.1039/c9nr09780e · Cited by 370 · see citing works
The Evolution of Extracellular Matrix
Özbek, S., Balasubramanian, P. G., Chiquet-Ehrismann, R., Tucker, R. P., & Adams, J. C. (2010) · Molecular Biology of the Cell · doi:10.1091/mbc.e10-03-0251 · Cited by 347 · see citing works
Design principles for creating synthetic underwater adhesives
Narayanan, A., Dhinojwala, A., & Joy, A. (2021) · Chemical Society Reviews · doi:10.1039/d1cs00316j · Cited by 193 · see citing works
Polydopamine-Assisted Surface Modification for Bone Biosubstitutes
Huang, S., Liang, N., Hu, Y., Zhou, X., & Abidi, N. (2016) · BioMed Research International · doi:10.1155/2016/2389895 · Cited by 97 · see citing works
- Authors
- Harrington, M. J., Masic, A., Holten-Andersen, N., Waite, J. H., & Fratzl, P.
- Affiliations
- Max Planck Institute of Colloids and Interfaces (DE)
- Department of Biomaterials, Max Planck Institute for Colloids and Interfaces, Potsdam 14424, Germany.
- Biomolecular Science and Engineering, University of California, Santa Barbara (UCSB), Santa Barbara, CA 93106, USA.
- University of California, Santa Barbara (US)
- Corresponding author
- Harrington, Matthew J.
- Venue
- Science
- Published
- 2010-04-09
- Volume
- 328
- Issue
- 5975
- Pages
- 216-220
- ISSN
- 0036-8075 (ISSN-L)
- 1095-9203
- PMC
- PMC3087814
- OpenAlex
- W2011556452
- Cited by
- 1,000
- References
- 1
- Citations by year
- 2026: 47 · 2025: 50 · 2024: 73 · 2023: 70 · 2022: 81 · 2021: 70 · 2020: 76 · 2019: 73 · 2018: 71 · 2017: 59 · 2016: 75 · 2015: 69 · 2014: 56 · 2013: 40 · 2012: 49
- FWCI
- 20.67
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- Science (publishedVersion)
- PubMed (publishedVersion)
- Europe PMC (PubMed Central) (acceptedVersion)
- PubMed Central (acceptedVersion)
- Max Planck Institute for Plasma Physics (submittedVersion)
- Max Planck Digital Library (submittedVersion)
- MPG.PuRe (Max Planck Society) (submittedVersion)
- Funders
- National Institute of Dental and Craniofacial Research (R01DE018468, R01DE015415)
- Topics
- Physical Sciences › Materials Science › Surfaces, Coatings and Films › Polymer Surface Interaction Studies
- Physical Sciences › Materials Science › Biomaterials › Calcium Carbonate Crystallization and Inhibition
- Physical Sciences › Engineering › Ocean Engineering › Marine Biology and Environmental Chemistry
- Keywords
- byssal threads, 3,4-dihydroxyphenylalanine, crosslinking, bioinspired coatings, Mytilidae
- MeSH terms
- Animals, Animal Structures, Biomechanical Phenomena, Dihydroxyphenylalanine, Ferric Compounds, Hardness, Iron, Models, Biological, Proteins, Spectrum Analysis, Raman, Repetitive Sequences, Amino Acid, Mytilus, Chemical Phenomena
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