Journal
ANGEWANDTE CHEMIE-INTERNATIONAL EDITION
Volume 59, Issue 42, Pages 18495-18499Publisher
WILEY-V C H VERLAG GMBH
DOI: 10.1002/anie.202008515
Keywords
adhesion; cohesion control; enzyme-induced polymerization; mussel glue; synthetic proteins
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Funding
- Alexander von Humboldt Foundation (AvH postdoctoral fellowship)
- DFG [GRK1865, BO1762/9-2]
- Austrian Science Fund (FWF) [P32326]
- Projekt DEAL
- Austrian Science Fund (FWF) [P32326] Funding Source: Austrian Science Fund (FWF)
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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 beta-sheets is suppressed by switch defects. This allows enzymatic activation and polymerization to proceed undisturbed. The beta-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 %.
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