A mussel-derived one component adhesive coacervate

Wei, Wei; Tan, YerPeng; Rodriguez, Nadine R. Martinez; Yu, Jing; Israelachvili, Jacob N.; Waite, J. Herbert

doi:10.1016/j.actbio.2013.09.007

Cited by 199 publications

(260 citation statements)

References 34 publications

(33 reference statements)

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“…112, Copyright 2014, with permission from Elsevier, and like‐charged polyelectrolytes facilitated by the strong short range cation–π interactions between catechol and cationic functional groups (C).…”

Section: Chemistry Of Adhesion: Mussel Adhesive Proteinsmentioning

confidence: 99%

Recent approaches in designing bioadhesive materials inspired by mussel adhesive protein

Forooshani

Lee

2016

J. Polym. Sci. Part A: Polym. Chem.

519

464

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Marine mussels secret protein‐based adhesives, which enable them to anchor to various surfaces in a saline, intertidal zone. Mussel foot proteins (Mfps) contain a large abundance of a unique, catecholic amino acid, Dopa, in their protein sequences. Catechol offers robust and durable adhesion to various substrate surfaces and contributes to the curing of the adhesive plaques. In this article, we review the unique features and the key functionalities of Mfps, catechol chemistry, and strategies for preparing catechol‐functionalized polymers. Specifically, we reviewed recent findings on the contributions of various features of Mfps on interfacial binding, which include coacervate formation, surface drying properties, control of the oxidation state of catechol, among other features. We also summarized recent developments in designing advanced biomimetic materials including coacervate‐forming adhesives, mechanically improved nano‐ and micro‐composite adhesive hydrogels, as well as smart and self‐healing materials. Finally, we review the applications of catechol‐functionalized materials for the use as biomedical adhesives, therapeutic applications, and antifouling coatings. © 2016 The Authors. Journal of Polymer Science Part A: Polymer Chemistry Published by Wiley Periodicals, Inc. J. Polym. Sci., Part A: Polym. Chem. 2017, 55, 9–33

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Section: Chemistry Of Adhesion: Mussel Adhesive Proteinsmentioning

confidence: 99%

Recent approaches in designing bioadhesive materials inspired by mussel adhesive protein

Forooshani

Lee

2016

J. Polym. Sci. Part A: Polym. Chem.

519

464

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“…Recent evidence [21] supports coacervate formation by one variant (mfp-3s) of the mfp family. In this case, the observed pores may be the solidified interface of the mfp-poor liquid drops dispersed in an mfp-rich continuous phase corresponding to the mesh network.…”

Section: Imaging Of Natural Plaquesmentioning

confidence: 99%

The microscopic network structure of mussel ( Mytilus ) adhesive plaques

Filippidi

DeMartini

Molina

et al. 2015

J. R. Soc. Interface.

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Marine mussels of the genus Mytilus live in the hostile intertidal zone, attached to rocks, bio-fouled surfaces and each other via collagen-rich threads ending in adhesive pads, the plaques. Plaques adhere in salty, alkaline seawater, withstanding waves and tidal currents. Each plaque requires a force of several newtons to detach. Although the molecular composition of the plaques has been well studied, a complete understanding of supra-molecular plaque architecture and its role in maintaining adhesive strength remains elusive. Here, electron microscopy and neutron scattering studies of plaques harvested from Mytilus californianus and Mytilus galloprovincialis reveal a complex network structure reminiscent of structural foams. Two characteristic length scales are observed characterizing a dense meshwork (approx. 100 nm) with large interpenetrating pores (approx. 1 mm). The network withstands chemical denaturation, indicating significant cross-linking. Plaques formed at lower temperatures have finer network struts, from which we hypothesize a kinetically controlled formation mechanism. When mussels are induced to create plaques, the resulting structure lacks a well-defined network architecture, showcasing the importance of processing over self-assembly. Together, these new data provide essential insight into plaque structure and formation and set the foundation to understand the role of plaque structure in stress distribution and toughening in natural and biomimetic materials.

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“…Similarly, mfp-3s showed dynamic microphase behavior at pH 3 to 7.5 at ionic strengths ≤ 100 mM. 8 We also studied phase behavior of the coacervate formed at pH 4 as a function of salt concentration. The copolymer started to precipitate above 100 mM salt where precipitation is attributed to decreasing the solvent quality (aq.…”

mentioning

confidence: 99%

“…1 Mfp-3s is localized to the plaque−substratum interface ( Figure 1b) together with mfp-3f and mfp-5. Due to its amphiphilic and ampholytic structural characteristics (Figure 2a), mfp-3s is capable of self-coacervation 8 and is more stable at oxidation than other mfps. 9 Intrigued by mfp-3s's (molecular weight ∼5 kDa) unique property to self-coacervate, we synthesized a series of ampholytic copolymers consisting of randomly arranged catechol (M1)-functionalized, cationic (M2), anionic (M3), nonionic hydrophilic (M4), and hydrophobic (M5) comonomer units (Figure 2b,c).…”

mentioning

confidence: 99%

Microphase Behavior and Enhanced Wet-Cohesion of Synthetic Copolyampholytes Inspired by a Mussel Foot Protein

Seo¹,

Das²,

Zalicki³

et al. 2015

J. Am. Chem. Soc.

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131

144

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Numerous attempts have been made to translate mussel adhesion to diverse synthetic platforms. However, the translation remains largely limited to the Dopa (3,4-dihydroxyphenylalanine) or catechol functionality, which continues to raise concerns about Dopa's inherent susceptibility to oxidation. Mussels have evolved adaptations to stabilize Dopa against oxidation. For example, in mussel foot protein 3 slow (mfp-3s, one of two electrophoretically distinct interfacial adhesive proteins in mussel plaques), the high proportion of hydrophobic amino acid residues in the flanking sequence around Dopa increases Dopa's oxidation potential. In this study, copolyampholytes, which combine the catechol functionality with amphiphilic and ionic features of mfp-3s, were synthesized and formulated as coacervates for adhesive deposition on surfaces. The ratio of hydrophilic/hydrophobic as well as cationic/anionic units was varied in order to enhance coacervate formation and wet adhesion properties. Aqueous solutions of two of the four mfp-3s-inspired copolymers showed coacervate-like spherical microdroplets (ϕ ≈ 1−5 μm at pH ∼4 (salt concentration ∼15 mM). The mfp-3s-mimetic copolymer was stable to oxidation, formed coacervates that spread evenly over mica, and strongly bonded to mica surfaces (pull-off strength: ∼17.0 mJ/m 2 ). Increasing pH to 7 after coacervate deposition at pH 4 doubled the bonding strength to ∼32.9 mJ/m 2 without oxidative cross-linking and is about 9 times higher than native mfp-3s cohesion. This study expands the scope of translating mussel adhesion from simple Dopa-functionalization to mimicking the context of the local environment around Dopa. M arine mussels (Figure 1a) attach to hard surfaces, e.g., mineral and metal, in the intertidal zone where waves with and without suspended sand often exceed 25 m/sec velocities. 3,4-Dihydroxyphenylalanine (Dopa), a main constituent in mussel foot proteins (mfps) and substantially contributing to wet adhesion, has been incorporated in synthetic polymers to mimic the bio wet-adhesion. 1−5 However, other constitutional features of mfps, e.g., cationic residues (lysine, K), anionic residues (aspartic acid, D), nonionic polar residues (asparagine, N), and nonpolar residues (alanine, A), have not typically been included in mussel-inspired synthetic wet-adhesion systems. 1,2Here, we studied the microphase behavior and wet-adhesion of copolyampholytes with fixed catechol content and varied other key functionalities. Potential effects of aromatic moieties (Tyr, Trp) besides Dopa in mfp-3s have not been specifically tested in the present structural design of the model copolyampholytes. Conditions for the experiments were adjusted according to the microenvironmental conditions of adhesive protein deposition under the mussel's foot including acidic to neutral pH and ionic strength of ≤100 mM. 3,4 In mussel adhesion, polyelectrolyte adhesive proteins or mfps are presented to target surfaces after being condensed as a dense fluid by complex coacervation, a critical ste...

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A mussel-derived one component adhesive coacervate

Cited by 199 publications

References 34 publications

Recent approaches in designing bioadhesive materials inspired by mussel adhesive protein

Recent approaches in designing bioadhesive materials inspired by mussel adhesive protein

The microscopic network structure of mussel ( Mytilus ) adhesive plaques

Microphase Behavior and Enhanced Wet-Cohesion of Synthetic Copolyampholytes Inspired by a Mussel Foot Protein

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