α,β-Dehydro-Dopa: A Hidden Participant in Mussel Adhesion

Mirshafian, Razieh; Wei, Wei; Israelachvili, Jacob N.; Waite, J. Herbert

doi:10.1021/acs.biochem.5b01177

Cited by 35 publications

(39 citation statements)

References 30 publications

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“…detectable solution structure at pH 3. Both Mfp-1 and Mfp-2 have local structure -such as polyproline II and an epidermal growth factor-like motif, respectively -connected by disordered sequences (Olivieri et al, 1997;Mirshafian et al, 2016). preCOLs are trimeric with supersecondary triple helical collagen cores flanked by silk-like β-sheets in preCOL-D, and disordered elastin in preCOL-P and preCOL-NG (Arnold et al, 2012).…”

Section: Lewis Basementioning

confidence: 99%

“…preCOLs are trimeric with supersecondary triple helical collagen cores flanked by silk-like β-sheets in preCOL-D, and disordered elastin in preCOL-P and preCOL-NG (Arnold et al, 2012). It is highly probable that a different structure is gained upon pH-induced precipitation, as for variants of Mfp-3 (Wei et al, 2013a;Mirshafian et al, 2016;Petrone et al, 2015), which gain β-sheet structure during titration from pH 3 to 7.5. …”

Section: Lewis Basementioning

confidence: 99%

“…Nine cysteine thiols and four Dopa residues contribute to the reservoir of reducing electrons, but little is known about the sequence of reactions involved, particularly the flow of electrons (Mirshafian et al, 2016). Many Mfp-6 thiol and Dopa residues have reducing redox potentials of about −0.22 and +0.25 V, respectively, that are capable of sacrificially reducing either O 2 or Dopa-quinones.…”

Section: Redoxmentioning

confidence: 99%

“…2Fii′-iii). At pH 6-8, in the presence of a Lewis base (see Glossary), electrons in the side-chain are recruited into the ring for quinone reduction back to catechol (Mirshafian et al, 2016). The new catechol, however, is no longer Dopa but a vinyl catechol known as α, β-dehydro (Δ)-Dopa (Rzepecki et al, 1991).…”

Section: Redoxmentioning

confidence: 99%

“…However, Δ-Dopa has an oxidation potential that is 100 mV more cathodic (easier to oxidize) than that of Dopa, and the formation of a vinylic double bond has consequences for protein conformation (Mirshafian et al, 2016). Probably, the oxidation of Δ-Dopa serves to add electrons to the reducing reservoir of Mfp-6 in a 'last ditch' effort to extend the lifetime of interfacial catechols and adhesion after which the plaque becomes obsolete (Mirshafian et al, 2016). Important questions about plaque redox are whether it ever equilibrates with seawater, and, if not, how a distinct redox environment is maintained in the plaque.…”

Section: Redoxmentioning

confidence: 99%

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Mussel adhesion – essential footwork

Waite

2017

Journal of Experimental Biology

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473

723

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Robust adhesion to wet, salt-encrusted, corroded and slimy surfaces has been an essential adaptation in the life histories of sessile marine organisms for hundreds of millions of years, but it remains a major impasse for technology. Mussel adhesion has served as one of many model systems providing a fundamental understanding of what is required for attachment to wet surfaces. Most polymer engineers have focused on the use of 3,4-dihydroxyphenyl-L-alanine (Dopa), a peculiar but abundant catecholic amino acid in mussel adhesive proteins. The premise of this Review is that although Dopa does have the potential for diverse cohesive and adhesive interactions, these will be difficult to achieve in synthetic homologs without a deeper knowledge of mussel biology; that is, how, at different length and time scales, mussels regulate the reactivity of their adhesive proteins. To deposit adhesive proteins onto target surfaces, the mussel foot creates an insulated reaction chamber with extreme reaction conditions such as low pH, low ionic strength and high reducing poise. These conditions enable adhesive proteins to undergo controlled fluid-fluid phase separation, surface adsorption and spreading, microstructure formation and, finally, solidification.

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Section: Lewis Basementioning

confidence: 99%

Section: Lewis Basementioning

confidence: 99%

Section: Redoxmentioning

confidence: 99%

Section: Redoxmentioning

confidence: 99%

Section: Redoxmentioning

confidence: 99%

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Mussel adhesion – essential footwork

Waite

2017

Journal of Experimental Biology

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473

723

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Bioinspired Underwater Adhesives by Using the Supramolecular Toolbox

et al. 2018

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several excellent reviews. [9][10][11][12] Recently, it was emphasized by Waite that catechol moieties alone are insufficient to ensure proper underwater adhesion and that the performance is a complex interplay between DOPA and its local environment. [13] Therefore, attention is shifted to include other (noncovalent) interactions used in these natural glues, and much progress has been made in understanding both their performance and delivery process. [14] In this review, we take the sandcastle worm and mussel as a basis for inspiration. We discuss (noncovalent) interactions found in these natural adhesive systems and extend our discussion to additional supramolecular moieties that can be used to control the adhesive and cohesive performance of synthetically designed adhesives. In Section 2, we examine the natural systems and identify the versatile supramolecular interactions used in such protein-based adhesives. These include electrostatic interactions, hydrogen bonding, hydrophobic forces, π-π interactions, metal coordination, cation-π complexation, and dynamic covalent linkages. The use of these interactions in synthetic adhesive systems is explored in the subsequent sections. Section 3 is devoted to the different interactions that catechols (the functional group of DOPA) display to bond to a submerged substrate or to provide cohesive properties to the adhesive. Despite the fact that catechols have already been the topic of many excellent reviews, [9,13,17] we believe that catechols play a pivotal role in both the sandcastle worm and the mussel adhesive systems and, therefore, should not be omitted from this review. In Section 4, we discuss the use of electrostatic interactions in protein-based and synthetic adhesive formulations for wet conditions. These interactions can be tailored to a wide distribution of bond strengths and thus can be tuned to change multi ple mechanical properties, which is essential for design of an adhesive. Besides the effect on the adhesive and cohesive properties, we highlight work where electrostatic interactions cause liquid-liquid phase separation in aqueous polymer solutions. The resulting (complex) coacervate is a concentrated, liquid, yet water-insoluble phase of the adhesive material, which can act as a powerful delivery tool for underwater adhesives. Hydrogen bonding in adhesives is explored in Section 5. The use of hydrogen bonding to adjust the viscoelastic properties of adhesives has been identified decades, ago, and hydrogen bonding moieties are commonly used in pressure sensitive adhesives (PSAs). However, besides simple, single hydrogen bonding motifs, many interesting alternative Nature has developed protein-based adhesives whose underwater performance has attracted much research attention over the last few decades. The adhesive proteins are rich in catechols combined with amphiphilic and ionic features. This combination of features constitutes a supramolecular toolbox, to provide stimuli-responsive processing of the adhesive, to secure strong adhesion to a variety of...

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Expanding the DOPA Universe with Genetically Encoded, Mussel‐Inspired Bioadhesives for Material Sciences and Medicine

Budiša

Schneider

2019

ChemBioChem

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Catechols are a biologically relevant group of aromatic diols that have attracted much attention as mediators of adhesion of “bio‐glue” proteins in mussels of the genus Mytilus. These organisms use catechols in the form of the noncanonical amino acid l‐3,4‐dihydroxyphenylalanine (DOPA) as a building block for adhesion proteins. The DOPA is generated post‐translationally from tyrosine. Herein, we review the properties, natural occurrence, and reactivity of catechols in the design of bioinspired materials. We also provide a basic description of the mussel's attachment apparatus, the interplay between its different molecules that play a crucial role in adhesion, and the role of post‐translational modifications (PTMs) of these proteins. Our focus is on the microbial production of mussel foot proteins with the aid of orthogonal translation systems (OTSs) and the use of genetic code engineering to solve some fundamental problems in the bioproduction of these bioadhesives and to expand their chemical space. The major limitation of bacterial expression systems is their intrinsic inability to introduce PTMs. OTSs have the potential to overcome these challenges by replacing canonical amino acids with noncanonical ones. In this way, PTM steps are circumvented while the genetically programmed precision of protein sequences is preserved. In addition, OTSs should enable spatiotemporal control over the complex adhesion process, because the catechol function can be masked by suitable chemical protection. Such caged residues can then be noninvasively unmasked by, for example, UV irradiation or thermal treatment. All of these features make OTSs based on genetic code engineering in reprogrammed microbial strains new and promising tools in bioinspired materials science.

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α,β-Dehydro-Dopa: A Hidden Participant in Mussel Adhesion

Cited by 35 publications

References 30 publications

Mussel adhesion – essential footwork

Mussel adhesion – essential footwork

Bioinspired Underwater Adhesives by Using the Supramolecular Toolbox

Expanding the DOPA Universe with Genetically Encoded, Mussel‐Inspired Bioadhesives for Material Sciences and Medicine

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