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search.filters.applied.f.access: openAccess × DDC: 540 × Type: Text × Publisher: Weinheim : Wiley-VCH × Subject: mussel glue × WGL Institute: IPF ×

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    Toward Artificial Mussel-Glue Proteins: Differentiating Sequence Modules for Adhesion and Switchable Cohesion
    (Weinheim : Wiley-VCH, 2020) Arias, Sandra; Amini, Shahrouz; Horsch, Justus; Pretzler, Matthias; Rompel, Annette; Melnyk, Inga; Sychev, Dmitrii; Fery, Andreas; Börner, Hans G.
    Artificial mussel-glue proteins with pH-triggered cohesion control were synthesized by extending the tyrosinase activated polymerization of peptides to sequences with specific modules for cohesion control. The high propensity of these sequence sections to adopt β-sheets is suppressed by switch defects. This allows enzymatic activation and polymerization to proceed undisturbed. The β-sheet formation is regained after polymerization by changing the pH from 5.5 to 6.8, thereby triggering O→N acyl transfer rearrangements that activate the cohesion mechanism. The resulting artificial mussel glue proteins exhibit rapid adsorption on alumina surfaces. The coatings resist harsh hypersaline conditions, and reach remarkable adhesive energies of 2.64 mJ m−2 on silica at pH 6.8. In in situ switch experiments, the minor pH change increases the adhesive properties of a coating by 300 % and nanoindentation confirms the cohesion mechanism to improve bulk stiffness by around 200 %. © 2020 The Authors. Published by Wiley-VCH GmbH
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    Polymerizing Like Mussels Do: Toward Synthetic Mussel Foot Proteins and Resistant Glues
    (Weinheim : Wiley-VCH, 2018) Horsch, Justus; Wilke, Patrick; Pretzler, Matthias; Seuss, Maximilian; Melnyk, Inga; Remmler, Dario; Fery, Andreas; Rompel, Annette; Börner, Hans G.
    A novel strategy to generate adhesive protein analogues by enzyme-induced polymerization of peptides is reported. Peptide polymerization relies on tyrosinase oxidation of tyrosine residues to Dopaquinones, which rapidly form cysteinyldopa-moieties with free thiols from cysteine residues, thereby linking unimers and generating adhesive polymers. The resulting artificial protein analogues show strong adsorption to different surfaces, even resisting hypersaline conditions. Remarkable adhesion energies of up to 10.9 mJ m−2 are found in single adhesion events and average values are superior to those reported for mussel foot proteins that constitute the gluing interfaces.