Metals and the Integrity of a Biological Coating: The Cuticle of Mussel Byssus

Holten‐Andersen, Niels; Mates, Thomas E.; Toprak, Muhammet S.; Stucky, Galen D.; Zok, Frank W.; Waite, J. Herbert

doi:10.1021/la8027012

Cited by 196 publications

(192 citation statements)

References 35 publications

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“…The cuticle is both hard and reversibly extensible up to 100% strain. 6,28 How these peculiar mechanical properties of the cuticle are related to mfp-1's unusual structure continues to intrigue. A variety of techniques have been performed to elucidate the structure of mfp-1.…”

Section: Discussionmentioning

confidence: 99%

“…In the byssal cuticle where mfp-1 is localized, a high concentration of Ca 2þ ions was also reported by secondary ion mass spectroscopy and the presence of various fatty acids (myristic acids, lauric acids, and palmitic acids) was proposed. 28 Therefore, Ca 2þ and the above-mentioned fatty acids were added separately or together to mfp-1 containing solutions. However, no detectable secondary structure changes in CD were evident (data not shown).…”

Section: (A)]mentioning

confidence: 99%

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Three intrinsically unstructured mussel adhesive proteins, mfp‐1, mfp‐2, and mfp‐3: Analysis by circular dichroism

Hwang

Waite

2012

Protein Science

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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 Ca 21 and Fe 31 . In contrast, mfp-2 exhibits Ca 21 -and disulfidestabilized 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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Section: Discussionmentioning

confidence: 99%

Section: (A)]mentioning

confidence: 99%

Three intrinsically unstructured mussel adhesive proteins, mfp‐1, mfp‐2, and mfp‐3: Analysis by circular dichroism

Hwang

Waite

2012

Protein Science

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“…Mfp-1 is a coating protein that forms the cuticle of the byssal plaque and thread ( Fig. 5b) [34,36,37]. Two variants of Mfp-1 exist and differ based on the exent of posttranslational hydroxylation of tyrosine to Dopa [33].…”

Section: Iron Coordination By Biological Catechols Catechol Siderophoresmentioning

confidence: 99%

“…When the cuticle is strained microcracks form preferentially within the softer surrounding protein matrix and these cracks extend until obstructed by a harder, 10 more highly crosslinked granule [33,34,36]. [49,50].…”

Section: Iron Coordination By Biological Catechols Catechol Siderophoresmentioning

confidence: 99%

Siderophores and mussel foot proteins: the role of catechol, cations, and metal coordination in surface adhesion

Maier

Butler

2017

J Biol Inorg Chem

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Metal coordination, hydrogen bonding, redox reactions, and covalent crosslinking are seemingly disparate chemical and physicochemical processes that are all accomplished in natural materials by the catechol functional group. This review focuses on the reactivity of catechols in tris-2,3-dihydroxybenzoyl-containing microbial siderophores and synthetic analogs, as well as Dopa-(3,4-dihydroxyphenylalanine)-containing mussel foot proteins that adhere to surfaces in aqueous conditions.Mussel foot proteins with a high content of Dopa and cationic amino acids, Lys and Arg, adhere strongly to mica, an aluminosilicate mineral, in aqueous conditions. The siderophore cyclic trichrysobactin, tris-(2,3-dihydroxybenzoyl-D-Lys-L-Ser) and related synthetic analogs in which the tri-Ser macrolactone is replaced by Tren, tris-(2-aminoethyl)amine, also adheres strongly to mica. Variation in the nature of the catechol and cationic groups in synthetic analogs reveals a synergism between the cationic amino acid and the catechol, required for strong aqueous adhesion. Autoxidation and iron(III)-catalyzed oxidation of 2,3-dihydroxy and 3,4-dihydroxy catechols is also considered. These siderophore analogs provide a platform to understand catechol interactions and reactivity on surfaces, which may ultimately improve the design of synthetic materials that address diverse challenges in medicine, materials science, as well as other disciplines, in which surface adhesion in aqueous conditions is important.

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“…temperature and pH) can lead to increased dislodgement in mussel beds [5]. The extensible fibrous core of the thread is coated by a thin protective cuticle (thickness 5-10 mm), which possesses hardness and stiffness values similar to epoxies, while at the same time exhibiting extensibility up to 100% before cracking (figure 1b) [6][7][8]. This unusual combination of high hardness/stiffness and extensibility is critical to the proposed abrasion-resistant function of the cuticle and was attributed largely to the presence of protein-metal cross-links organized in a hierarchical particlereinforced composite-like structure (figure 1b,c) [6,8,9].…”

Section: Introductionmentioning

confidence: 99%

Mechanical homeostasis of a DOPA-enriched biological coating from mussels in response to metal variation

Schmitt

Winter

Bertinetti

et al. 2015

J. R. Soc. Interface.

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Protein -metal coordination interactions were recently found to function as crucial mechanical cross-links in certain biological materials. Mussels, for example, use Fe ions from the local environment coordinated to DOPA-rich proteins to stiffen the protective cuticle of their anchoring byssal attachment threads. Bioavailability of metal ions in ocean habitats varies significantly owing to natural and anthropogenic inputs on both short and geological spatio-temporal scales leading to large variations in byssal thread metal composition; however, it is not clear how or if this affects thread performance. Here, we demonstrate that in natural environments mussels can opportunistically replace Fe ions in the DOPA coordination complex with V and Al. In vitro removal of the native DOPA-metal complexes with ethylenediaminetetraacetic acid and replacement with either Fe or V does not lead to statistically significant changes in cuticle performance, indicating that each metal ion is equally sufficient as a DOPA cross-linking agent, able to account for nearly 85% of the stiffness and hardness of the material. Notably, replacement with Al ions also leads to full recovery of stiffness, but only 82% recovery of hardness. These findings have important implications for the adaptability of this biological material in a dynamically changing and unpredictable habitat.

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Metals and the Integrity of a Biological Coating: The Cuticle of Mussel Byssus

Cited by 196 publications

References 35 publications

Three intrinsically unstructured mussel adhesive proteins, mfp‐1, mfp‐2, and mfp‐3: Analysis by circular dichroism

Three intrinsically unstructured mussel adhesive proteins, mfp‐1, mfp‐2, and mfp‐3: Analysis by circular dichroism

Siderophores and mussel foot proteins: the role of catechol, cations, and metal coordination in surface adhesion

Mechanical homeostasis of a DOPA-enriched biological coating from mussels in response to metal variation

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