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

Hwang, Dong Soo; Waite, J. Herbert

doi:10.1002/pro.2147

Cited by 60 publications

(43 citation statements)

References 44 publications

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“…By contrast, mfp-3 is an adhesive primer for mussel adhesion and it should have underwater adhesion ability regardless of surface chemistry. Recent studies aided by SFG vibrational spectroscopy and CD strongly support the notion that mfp-3 adopts different conformations at various interfaces depending on specific chemical interactions [41][42][43]. Therefore, relatively stronger adhesion ability of mfp-3 to the tested substrates than mfp-1 and mfp-5 is partially due to a superior conformational adaptability of mfp-3 on the different surface chemistries.…”

Section: Psmentioning

confidence: 85%

Adhesion of mussel foot proteins to different substrate surfaces

Danner

Waite

et al. 2013

J. R. Soc. Interface.

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Mussel foot proteins (mfps) have been investigated as a source of inspiration for the design of underwater coatings and adhesives. Recent analysis of various mfps by a surface forces apparatus (SFA) revealed that mfp-1 functions as a coating, whereas mfp-3 and mfp-5 resemble adhesive primers on mica surfaces. To further refine and elaborate the surface properties of mfps, the force-distance profiles of the interactions between thin mfp (i.e. mfp-1, mfp-3 or mfp-5) films and four different surface chemistries, namely mica, silicon dioxide, polymethylmethacrylate and polystyrene, were measured by an SFA. The results indicate that the adhesion was exquisitely dependent on the mfp tested, the substrate surface chemistry and the contact time. Such studies are essential for understanding the adhesive versatility of mfps and related/similar adhesion proteins, and for translating this versatility into a new generation of coatings and (including in vivo) adhesive materials.

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Section: Psmentioning

confidence: 85%

Adhesion of mussel foot proteins to different substrate surfaces

Danner

Waite

et al. 2013

J. R. Soc. Interface.

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281

243

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“…It is hypothesized that Mfp-3′s increased adhesion over both Mfp-1 and Mfp-5 is a result of the marked asymmetric distribution of hydrophobic tryptophans along the protein length; with the predominantly hydrophobic C terminus of Mfp-3 adsorbed at the CH-SAM interface, the remainder of the molecule is more mobile to scavenge Dopa-mediated binding sites at the mica interface. This effect may be enhanced by Mfp3′s high degree of chain flexibility (17). Preferential distribution of hydrophobic moieties toward either terminus of a peptide sequence is believed to be a favorable criterion for designing proteins with maximum adhesion between chemically heterogeneous interfaces.…”

Section: Mfp-1mentioning

confidence: 99%

Adaptive hydrophobic and hydrophilic interactions of mussel foot proteins with organic thin films

Yu¹,

Kan

Rapp³

et al. 2013

Proc. Natl. Acad. Sci. U.S.A.

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The adhesion of mussel foot proteins (Mfps) to a variety of specially engineered mineral and metal oxide surfaces has previously been investigated extensively, but the relevance of these studies to adhesion in biological environments remains unknown. Most solid surfaces exposed to seawater or physiological fluids become fouled by organic conditioning films and biofilms within minutes. Understanding the binding mechanisms of Mfps to organic films with known chemical and physical properties therefore is of considerable theoretical and practical interest. Using selfassembled monolayers (SAMs) on atomically smooth gold substrates and the surface forces apparatus, we explored the forcedistance profiles and adhesion energies of three different Mfps, Mfp-1, Mfp-3, and Mfp-5, on (i) hydrophobic methyl (CH 3 )-and (ii) hydrophilic alcohol (OH)-terminated SAM surfaces between pH 3 and pH 7.5. At acidic pH, all three Mfps adhered strongly to the CH 3 -terminated SAM surfaces via hydrophobic interactions (range of adhesive interaction energy = −4 to −9 mJ/m 2 ) but only weakly to the OH-terminated SAM surfaces through H-bonding (adhesive interaction energy ≤ −0.5 mJ/m 2 ). 3, 4-Dihydroxyphenylalanine (Dopa) residues in Mfps mediate binding to both SAM surface types but do so through different interactions: typical bidentate H-bonding by Dopa is frustrated by the longer spacing of OHSAMs; in contrast, on CH 3 -SAMs, Dopa in synergy with other nonpolar residues partitions to the hydrophobic surface. Asymmetry in the distribution of hydrophobic residues in intrinsically unstructured proteins, the distortion of bond geometry between H-bonding surfaces, and the manipulation of physisorbed binding lifetimes represent important concepts for the design of adhesive and nonfouling surfaces. M arine mussels are experts at wet adhesion, achieving strong and durable attachments to a variety of surfaces in their chemically heterogeneous habitat. Adhesion is mediated by a byssus, which is essentially a bundle of leathery threads that emerge from the living mussel tissue at one end and are tipped by flat adhesive plaques at the other. Byssal plaques consist of a complex array of proteins (mostly mussel foot proteins, Mfps), each of which has a distinct localization and function in the structure, but all share the unusual modified amino acid 3, 4-dihydroxyphenylalanine (Dopa) (Fig. 1).Of the dozen or so known mussel foot proteins, Mfp-1, Mfp-3, and Mfp-5 have been shown to exhibit remarkable binding to mineral surfaces such as mica and TiO 2 (1). The versatility of mussel adhesion to surfaces with wide-ranging chemical and physical properties has inspired much research dedicated to understanding the mechanism of mussel adhesion and to developing biomimetic coatings and adhesives for wide-ranging industrial and biomedical applications, the latter including paints for coronary arteries (2), fetal membrane sealants (3), cell encapsulants (4), bone glues (5), and for securing transplants for diabetics (6).The catecholic moiety of Dopa (Fig. 1) ...

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“…In the plaque, we do not expect the proteins to behave as if they were fully solvated polymers or denatured proteins, as there is a large degree of cross-linking, hydrogen bonding, disulfide bonding and possibly metal coordination structuring them. Also, the proteins are not in a collapsed, globular state, corresponding to v ¼ 0.38 [31], as they are known to be disordered or with disordered sections [14]; thus the value of v is limited to the range 0.4-0.588. Here, v ¼ 0.5 is chosen as the most reasonable Flory exponent.…”

Section: Scattering Of Natural Plaquesmentioning

confidence: 99%

“…Plaque cohesion has been shown to partly arise from enhanced hydrogen bonding and metal coordination enabled by the abundant catecholic side groups of 3,4-dihydroxyphenyl-L-alanine (DOPA) in the mfps [12] in conjunction with catechol oxidase-mediated protein cross-linking [13]. Mussel foot proteins mfp-1, -2, -3, -4, -5, -6 have been purified and extensively studied and mfps-1, -2 and -3 have been shown to be intrinsically disordered or have disordered domains [14] with possible advantages for plaque processing and assembly. The role of these proteins in energy dissipation is not yet understood.…”

Section: Introductionmentioning

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

Cited by 60 publications

References 44 publications

Adhesion of mussel foot proteins to different substrate surfaces

Adhesion of mussel foot proteins to different substrate surfaces

Adaptive hydrophobic and hydrophilic interactions of mussel foot proteins with organic thin films

The microscopic network structure of mussel ( Mytilus ) adhesive plaques

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