Cross-linking of DOPA-proteins in the eggshell of Bdelloura candida, a marine worm: a PIXE study

Swann, C.P.; Waite, J. Herbert; Huggins, Luke G.

doi:10.1016/0168-583x(95)01214-1

Cited by 5 publications

(4 citation statements)

References 6 publications

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“…If low pH is a precaution limited to Dopa-based protein adhesives, then it may be imposed during adhesion by sandcastle worms (Waite et al 1992), cnidarian hydroids (Hwang et al 2013), turbellarians (Swann et al 1996) and tunicates (Dorsett et al 1987), all of which are known to use Dopa-proteins. If more widely practiced, it may offer a significant potential control point against biofouling that has not previously been considered.…”

Section: Discussionmentioning

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: Discussionmentioning

confidence: 99%

Interfacial pH during mussel adhesive plaque formation

et al. 2015

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“…Another natural example is the marine worm Bdelloura candida, producing a dopa-protein, which is believed to contribute to the curing of the primary inner layer of its eggshell. 120,121 During the hardening and darkening of the eggshell, the metal levels (e.g., iron, copper, zinc, and lead) increase, suggesting the occurrence of a metal-dependent curing process.…”

Section: Role Of Metal Ions In Adhesive Curingmentioning

confidence: 99%

Jack of all trades: versatile catechol crosslinking mechanisms

2014

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Catechols play an important role in many natural systems. They are known to readily interact with both organic (e.g., amino acids) and inorganic (e.g., metal ions, metal oxides) compounds, thereby providing a powerful system for protein curing. Catechol crosslinked protein networks, such as sclerotized cuticle and byssal threads of the mussel, have been shown to exhibit excellent mechanical properties. A lot of effort has been devoted to mimicking the natural proteins using synthetic catechol-functionalized polymers. Despite the success in developing catechol-functionalized materials, the crosslinking chemistry of catechols is still a subject of debate. To develop materials with controlled and superior properties, a clear understanding of the crosslinking mechanism of catechols is of vital importance. This review describes the crosslinking pathways of catechol and derivatives in both natural and synthetic systems. We discuss existing pathways of catechol crosslinking and parameters that affect the catechol chemistry in detail. This overview will point towards a rational direction for further investigation of the complicated catechol chemistry.

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“…The marine worm Bdelloura candida produces a DOPA-protein believed to be involved in curing of the primary, inner layer of its eggshells. 19,20 Hardening and darkening of the eggshell is accompanied by increased metal levels (e.g., iron, copper, zinc, and lead), thereby suggesting that metal-dependent cross-linking processes may be occurring. 19 Ascidians produce a number of DOPA-proteins that are suggested to participate in material formation functions such as generating wound plugs for tunic repair.…”

Section: Introductionmentioning

confidence: 99%

“…19,20 Hardening and darkening of the eggshell is accompanied by increased metal levels (e.g., iron, copper, zinc, and lead), thereby suggesting that metal-dependent cross-linking processes may be occurring. 19 Ascidians produce a number of DOPA-proteins that are suggested to participate in material formation functions such as generating wound plugs for tunic repair. 15,17 The common blue mussel, Mytilus edulis, may use the metal binding properties of protein-bound DOPA for construction of its impressively strong marine adhesive.…”

Section: Introductionmentioning

confidence: 99%

Absorption spectroscopy and binding constants for first-row transition metal complexes of a DOPA-containing peptide

2006

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A diverse array of biological systems incorporate 3,4-dihydroxyphenlyalanine (DOPA) into proteins and small molecules for cross-linking and material generation. Marine worm eggshells, sea squirt wound plugs, and marine mussel adhesives may all be formed by combining DOPA-containing molecules with high levels of metals. In order to provide model systems for characterizing these biomaterials, we carried out a study on metal binding to a DOPA-containing peptide. Ultraviolet-visible absorption spectra are presented for the AdopaTP peptide binding to Fe3+, V3+, VO2+, Mn3+, Ti4+, Cu2+, Co2+, and Ni2+ in mono, bis, and where applicable, tris coordination modes. Association constants were determined for selected metal ions binding to the peptide. In general, the spectroscopic and binding properties of this DOPA-containing peptide were found to be similar to those of catechol.

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Cross-linking of DOPA-proteins in the eggshell of Bdelloura candida, a marine worm: a PIXE study

Cited by 5 publications

References 6 publications

Interfacial pH during mussel adhesive plaque formation

Interfacial pH during mussel adhesive plaque formation

Jack of all trades: versatile catechol crosslinking mechanisms

Absorption spectroscopy and binding constants for first-row transition metal complexes of a DOPA-containing peptide

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