[1] Precursors of quinone tanning: Dopa-containing proteins

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    • Marine hydroid perisarc: A chitin- and melanin-reinforced composite with DOPA-iron(III) complexes

      2013, Acta Biomaterialia
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      The proximal end of a rachis, where the hydroid polyp holdfast is tethered to the substratum, was also stained red with Arnow, implying that the hydroid may utilize DOPA in underwater adhesive proteins, as mussels and sandcastle worms do. Whole hydroids were homogenized in 8 M urea/5% acetic acids, then the supernatant was separated in acid–urea polyacrylamide gel electrophoresis gel and stained with Coomassie blue R and nitroblue tetrazolium (NBT) to detect DOPA-containing protein (Fig. S2) [29]. A cluster of NBT-positive bands are detected and provide evidence for the existence of DOPA-containing protein in the hydroids.

    • Biological materials: Functional adaptations and bioinspired designs

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      The answer seems to lie in the presence (30 mol%) of 3,4-dihydroxyl phenylanine (DOPA) in the plaque. Underwater adhesion has been shown to be strongly correlated to the presence of a high DOPA content in the adhesive plaques of the mussels [507–509]. The critical role of DOPA on molecular-scale adhesion was demonstrated by Lee et al. [480] who performed single-molecule force type experiments with an AFM tip functionalized with DOPA.

    • Schistosoma mansoni: The egg, biosynthesis of the shell and interaction with the host

      2012, Experimental Parasitology
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      This cross-linking within a single protein and between neighboring proteins, results in an extensively cross-linked protein matrix. The appearance of the o-quinones leads to a rapid change in color and hardening of the proteins, rendering them intractable to all protease activity and only hydrolytic treatments can dissolve the cross-linked eggshell (Waite, 1995). The cross-linked eggshells are highly fluorescent.

    • Molecular interactions of mussel protective coating protein, mcfp-1, from Mytilus californianus

      2012, Biomaterials
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      The mcfp-1 containing fractions were pooled and polished by C8 reverse-phase HPLC using an acetonitrile gradient in water with 0.1% trifluoroacetic acid. Mcfp-1 eluted at about 22% acetonitrile [23]. Following HPLC, the proteins were freeze-dried and stored at −80 °C in vacuumed glass vial to prevent oxidation of DOPA.

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