Mussel protein adhesion depends on interprotein thiol-mediated redox modulation

Yu, Jing; Wei, Wei; Danner, Eric; Ashley, Rebekah K.; Israelachvili, Jacob N.; Waite, J. Herbert

doi:10.1038/nchembio.630

Cited by 396 publications

(508 citation statements)

References 25 publications

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“…Fresh byssal threads were induced by injecting the foot of the mussel with potassium chloride, a method that has been used extensively in marine mussels (Tamarin et al 1976;Zhao & Waite 2006;Yu et al 2011), but not in freshwater mussels. In marine mussels, the induced byssal threads were shown to be very similar in composition to natural threads (Sagert & Waite 2009;Yu et al 2011).…”

Section: Introductionmentioning

confidence: 99%

Byssal proteins of the freshwater zebra mussel,Dreissena polymorpha

2012

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The freshwater zebra mussel (Dreissena polymorpha) is a notorious biofouling organism. It adheres to a variety of substrata underwater by means of a proteinaceous structure called the byssus, which consists of a number of threads with adhesive plaques at the tips. The byssal proteins are difficult to characterize due to extensive cross-linking of 3,4-dihydroxyphenylalanine (DOPA), which renders the mature structure largely resistant to protein extraction and immunolocalization. By inducing secretion of fresh threads and plaques in which cross-linking is minimized, three novel zebra mussel byssal proteins were identified following extraction and separation by gel electrophoresis. Peptide fragment fingerprinting was used to match tryptic digests of several gel bands against a cDNA library of genes expressed uniquely in the mussel foot, the organ which secretes the byssus. This allowed identification of a more complete sequence of Dpfp2 (D. polymorpha foot protein 2), a known DOPA-containing byssal protein, and a partial sequence of Dpfp5, a novel protein with several typical characteristics of mussel adhesive proteins.

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Section: Introductionmentioning

confidence: 99%

Byssal proteins of the freshwater zebra mussel,Dreissena polymorpha

2012

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“…Mussel adhesive holdfasts exhibit significant self-healing capabilities 11,12 , although the molecular mechanisms involved are poorly understood. Notwithstanding this, the selfmending adhesion and cohesion of isolated dopa (3,4-dihydroxyphenyl-L-alanine)-containing adhesive proteins were shown to rely critically on maintaining dopa in an acidic and reducing environment 13,14 . Significantly different conditions are required to recapitulate the self-healing cohesion of tris-dopa-Fe 3+ -mediated complexes in proteins and polymers [7][8][9]15 .…”

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confidence: 99%

“…Previous studies have proposed that the self-healing adhesion of catechol-functionalized polymers and proteins relies on the bidentate hydrogen bonding of catechols as well as on hydrophobic contributions 13,20,28 . If the same is true for catecholic polyacrylates, then molecular and polymer mobility should be important contributing factors.…”

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confidence: 99%

Surface-initiated self-healing of polymers in aqueous media

et al. 2014

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Polymeric materials that intrinsically heal at damage sites under wet or moist conditions are urgently needed for biomedical and environmental applications [1][2][3][4][5][6] . Although hydrogels with self-mending properties have been engineered by means of mussel-inspired metal-chelating catechol-functionalized polymer networks 7-10 , biological self-healing in wet conditions, as occurs in self-assembled holdfast proteins in mussels and other marine organisms 11,12 , is generally thought to involve more than reversible metal chelates. Here we demonstrate self-mending in metal-free water of synthetic polyacrylate and polymethacrylate materials that are surface-functionalized with mussel-inspired catechols. Wet self-mending of scission in these polymers is initiated and accelerated by hydrogen bonding between interfacial catechol moieties, and consolidated by the recruitment of other non-covalent interactions contributed by subsurface moieties. The repaired and pristine samples show similar mechanical properties, suggesting that the triggering of complete self-healing is enabled underwater by the formation of extensive catechol-mediated interfacial hydrogen bonds.All polymeric materials suffer damage in the course of their functional lifetimes. Few, if any, completely heal at damage sites. Despite recent progress in the design of self-mending polymeric materials based on crack-activated crosslinking 1 , light 2 , heat 3 or other external stimuli 4 , these remain less than perfectly healed, and, in the case of polymers in wet environments, self-healing technologies are even more limited than those engineered for dry conditions. Mussel adhesive holdfasts exhibit significant self-healing capabilities 11,12 , although the molecular mechanisms involved are poorly understood. Notwithstanding this, the selfmending adhesion and cohesion of isolated dopa (3,4-dihydroxyphenyl-L-alanine)-containing adhesive proteins were shown to rely critically on maintaining dopa in an acidic and reducing environment 13,14 . Significantly different conditions are required to recapitulate the self-healing cohesion of tris-dopa-Fe 3+ -mediated complexes in proteins and polymers [7][8][9]15 . Such results increasingly suggest the importance of dopa, but also its subtle and diverse interfacial reactivity vis-à-vis the traditional and still widely held view that dopa, and catechols generally, function primarily as crosslinkers after their 2-electron oxidation to quinones 16 . To better assess the contribution of catechol to polymer selfhealing in a reducing (pH 3), metal-free wet environment, we prepared a material from common, water-insoluble synthetic acrylic polymers having a catechol-functionalized surface. These materials are completely self-healing in a process initiated by catecholmediated interfacial hydrogen bonding, and consolidated by followup interactions (for example, hydrophobic and steric) after a brief compression (∼6 × 10 4 Pa). The crucial and robust roles played by

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“…Indeed, earlier work has explored properties of dihydroxyphenylalanine as a key adhesion protein, found at the end of a byssus thread's adhesion plaque (Fig. 1b) 4,6,7,[10][11][12][13] . Unlike other species such as affixed barnacles, mussels dangle at a distance from the substrate and their connection is provided by the network of byssus threads.…”

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confidence: 99%

Impact tolerance in mussel thread networks by heterogeneous material distribution

Qin

Buehler

2013

Nat Commun

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The Mytilidae, generally known as marine mussels, are known to attach to most substrates including stone, wood, concrete and iron by using a network of byssus threads. Mussels are subjected to severe mechanical impacts caused by waves. However, how the network of byssus threads keeps the mussel attached in this challenging mechanical environment is puzzling, as the dynamical forces far exceed the measured strength of byssus threads and their attachment to the environment. Here we combine experiment and simulation, and show that the heterogeneous material distribution in byssus threads has a critical role in decreasing the effect of impact loading. We find that a combination of stiff and soft materials at an 80:20 ratio enables mussels to rapidly and effectively dissipate impact energy. Notably, this facilitates a significantly enhanced strength under dynamical loading over 900% that of the strength under static loading.

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Mussel protein adhesion depends on interprotein thiol-mediated redox modulation

Cited by 396 publications

References 25 publications

Byssal proteins of the freshwater zebra mussel,Dreissena polymorpha

Byssal proteins of the freshwater zebra mussel,Dreissena polymorpha

Surface-initiated self-healing of polymers in aqueous media

Impact tolerance in mussel thread networks by heterogeneous material distribution

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