Mussel adhesive protein provides cohesive matrix for collagen type-1α

Rodriguez, Nadine R. Martinez; Das, Saurabh; Kaufman, Yair; Wei, Wei; Israelachvili, Jacob N.; Waite, J. Herbert

doi:10.1016/j.biomaterials.2015.01.033

Cited by 41 publications

(32 citation statements)

References 24 publications

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“…The pH-sensitivity of 3,4-dihydroxyphenylalanine (Dopa) oxidation is an excellent case in point. Mfps such as mfp-3 and mfp-5 contain 20-30 mol% Dopa and are highly adhesive (eg E adh = -14 mJ m −2 on mica) within narrowly defined solution conditions (Danner et al 2012, Nicklisch et al 2013; Martinez Rodriguez et al 2015). Increasing the pH of mfp deposition in vitro from ~3 to 7.5, for example, typically causes significant Dopa oxidation and abolishes mfp-3 and -5 adhesion to mica, which is counterintuitive given that the ambient seawater around natural mussel clusters has a pH of ~8.…”

Section: Introductionmentioning

confidence: 99%

Interfacial pH during mussel adhesive plaque formation

et al. 2015

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Mussel (Mytilus californianus) adhesion to marine surfaces involves an intricate and adaptive synergy of molecules and spatio-temporal processes. Although the molecules, such as mussel foot proteins (mfps), are well characterized, deposition details remain vague and speculative. Developing methods for the precise surveillance of conditions that apply during mfp deposition would aid both in understanding mussel adhesion and translating this adhesion into useful technologies. To probe the interfacial pH at which mussels buffer the local environment during mfp deposition, a lipid bilayer with tethered pH-sensitive fluorochromes was assembled on mica. The interfacial pH during foot contact with modified mica ranged from 2.2−3.3, which is well below the seawater pH of ~8. The acidic pH serves multiple functions: it limits mfp-Dopa oxidation, thereby enabling the catecholic functionalities to adsorb to surface oxides by H-bonding and metal ion coordination, and provides a solubility switch for mfps, most of which aggregate at pH ≥ 7-8.

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Section: Introductionmentioning

confidence: 99%

Interfacial pH during mussel adhesive plaque formation

et al. 2015

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“…Although the role of Dopa in wet adhesion is under increasing scrutiny, its introduction into polymers often endows them with strong underwater adhesion 2 4 5 and self-healing 6 7 8 capabilities. Other common amino acids, for example, lysine, phosphoserine and histidine, are also relevant to mfp adhesion 9 10 and merit translation to synthetic systems 4 11 . Mfps are protein polyelectrolytes with high charge densities 12 , and lend themselves to complex coacervation, which appears to be critical for the lossless fluidic delivery of mfps to target surfaces underwater 9 12 .…”

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High-performance mussel-inspired adhesives of reduced complexity

et al. 2015

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Despite the recent progress in and demand for wet adhesives, practical underwater adhesion remains limited or non-existent for diverse applications. Translation of mussel-inspired wet adhesion typically entails catechol functionalization of polymers and/or polyelectrolytes, and solution processing of many complex components and steps that require optimization and stabilization. Here we reduced the complexity of a wet adhesive primer to synthetic low-molecular-weight catecholic zwitterionic surfactants that show very strong adhesion (∼50 mJ m−2) and retain the ability to coacervate. This catecholic zwitterion adheres to diverse surfaces and self-assembles into a molecularly smooth, thin (<4 nm) and strong glue layer. The catecholic zwitterion holds particular promise as an adhesive for nanofabrication. This study significantly simplifies bio-inspired themes for wet adhesion by combining catechol with hydrophobic and electrostatic functional groups in a small molecule.

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“…Understanding these differences will help inspire the design of future biomimetic polymers or recombinant mfp-1 proteins for biomedical and functional coatings for wet adhesion and friction applications. 21–25 …”

Section: Introductionmentioning

confidence: 99%

Tough Coating Proteins: Subtle Sequence Variation Modulates Cohesion

Das¹,

Miller²,

Kaufman³

et al. 2015

Biomacromolecules

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Mussel foot protein-1 (mfp-1) is an essential constituent of the protective cuticle covering all exposed portions of the byssus (plaque and the thread) that marine mussels use to attach to intertidal rocks. The reversible complexation of Fe3+ by the 3,4-dihydroxyphenylalanine (Dopa) side chains in mfp-1 in Mytilus californianus cuticle is responsible for its high extensibility (120%) as well as its stiffness (2 GPa) due to the formation of sacrificial bonds that help to dissipate energy and avoid accumulation of stresses in the material. We have investigated the interactions between Fe3+ and mfp-1 from two mussel species, M. californianus (Mc) and M. edulis (Me), using both surface sensitive and solution phase techniques. Our results show that although mfp-1 homologues from both species bind Fe3+, mfp-1 (Mc) contains Dopa with two distinct Fe3+-binding tendencies and prefers to form intramolecular complexes with Fe3+. In contrast, mfp-1 (Me) is better adapted to intermolecular Fe3+ binding by Dopa. Addition of Fe3+ did not significantly increase the cohesion energy between the mfp-1 (Mc) films at pH 5.5. However, iron appears to stabilize the cohesive bridging of mfp-1 (Mc) films at the physiologically relevant pH of 7.5, where most other mfps lose their ability to adhere reversibly. Understanding the molecular mechanisms underpinning the capacity of M. californianus cuticle to withstand twice the strain of M. edulis cuticle is important for engineering of tunable strain tolerant composite coatings for biomedical applications.

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Mussel adhesive protein provides cohesive matrix for collagen type-1α

Cited by 41 publications

References 24 publications

Interfacial pH during mussel adhesive plaque formation

Interfacial pH during mussel adhesive plaque formation

High-performance mussel-inspired adhesives of reduced complexity

Tough Coating Proteins: Subtle Sequence Variation Modulates Cohesion

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