Extra‐Organismic Adhesive Proteins

Lucas, Jared M.; Vaccaro, Eleonora; Waite, J. Herbert

doi:10.1002/3527600035.bpol8013

Cited by 8 publications

(13 citation statements)

References 104 publications

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“…2 Waite and coworkers discovered that the byssal thread is composed primarily of specialized collagen proteins (PreCol proteins) that contain domains with a high content of histidine (13–19 %) and sequence homology amongst species. 5–8 Histidine, an amino acid that is often involved in metal ion coordination in proteins, is hypothesized to bind metal ions such as Zn 2+ and Cu 2+ in the byssal thread, whereupon the metal coordination bond is thought to break under applied load, serving as an energy dissipating mechanism. 9 Unlike most covalent bonds whose rupture is generally irreversible, coordinate bonds are capable of reforming after rupture, i.e., functioning as sacrificial bonds.…”

Section: Introductionmentioning

confidence: 99%

Mussel-Inspired Histidine-Based Transient Network Metal Coordination Hydrogels

et al. 2013

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Transient network hydrogels cross-linked through histidine-divalent cation coordination bonds were studied by conventional rheologic methods using histidine-modified star poly(ethylene glycol) (PEG) polymers. These materials were inspired by the mussel, which is thought to use histidine-metal coordination bonds to impart self-healing properties in the mussel byssal thread. Hydrogel viscoelastic mechanical properties were studied as a function of metal, pH, concentration, and ionic strength. The equilibrium metal-binding constants were determined by dilute solution potentiometric titration of monofunctional histidine-modified methoxy-PEG and were found to be consistent with binding constants of small molecule analogs previously studied. pH-dependent speciation curves were then calculated using the equilibrium constants determined by potentiometric titration, providing insight into the pH dependence of histidine-metal ion coordination and guiding the design of metal coordination hydrogels. Gel relaxation dynamics were found to be uncorrelated with the equilibrium constants measured, but were correlated to the expected coordination bond dissociation rate constants.

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Section: Introductionmentioning

confidence: 99%

Mussel-Inspired Histidine-Based Transient Network Metal Coordination Hydrogels

et al. 2013

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“…Indeed, an earlier study also concluded this for the mechanical properties of byssal threads from Mytilus complex species. 31 …”

Section: Methodsmentioning

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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“…have life histories that depend on their secure attachment to solid substrates for survival. These organisms produce and secrete adhesive proteins that form permanent, strong, and flexible underwater bonds to a variety of substrates, such as glass, Teflon, metal, and plastic 4–6. Likewise, algae are known for their ability to settle, adhere, and proliferate on virtually any exposed surface 6.…”

Section: Introductionmentioning

confidence: 99%

Structure of Algal‐Born Phenolic Polymeric Adhesives

Bitton

Ben-Yehuda

Davidovich

et al. 2006

Macromolecular Bioscience

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Adhesive materials extracted from the brown alga Fucus serratus are composed of phenolic polymer, alginate, and CaCl2. The phenolic polymer undergoes an oxidation reaction in the presence of bromoperoxidase, KI, and H2O2. The nanostructure of the adhesive was investigated using small angle X-ray scattering, light scattering, and cryo- transmission electron microscopy experiments. These have shown that the phenolic polymer undergoes self-assembly and forms flexible chain-like objects. Oxidation or adding alginate does not alter this structure. However, once calcium ions are added, a rigid network is formed. Presumably, this network is responsible for the cohesive strength of the glue.

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Extra‐Organismic Adhesive Proteins

Abstract: Introduction Occurrence Barnacles Algae Mussels Molecular Genetics Functional Biomechanics Measurement of Adhesion Strength Applications of Mussel Adhesive Proteins Mucoadhesion and Surface Ch… Show more

Cited by 8 publications

References 104 publications

Mussel-Inspired Histidine-Based Transient Network Metal Coordination Hydrogels

Mussel-Inspired Histidine-Based Transient Network Metal Coordination Hydrogels

Tough Coating Proteins: Subtle Sequence Variation Modulates Cohesion

Structure of Algal‐Born Phenolic Polymeric Adhesives

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