Implementing Zn ion and pH-value control into artificial mussel glue proteins by abstracting a His-rich domain from preCollagen

A His-rich domain of preCollagen-D found in byssal threads is derivatized with Cys and Dopa flanks to allow for mussel-inspired polymerization. Artificial mussel glue proteins are accessed that combine cysteinyldopa for adhesion with sequences for pH or Zn 2+ induced β-sheet formation. The artificial constructs show strong adsorption to Al 2 O 3 , the resulting coatings tolerate hypersaline conditions and cohesion is improved by activating the β-sheet formation, that enhances E-modulus up to 60%. A chemically activated mussel-inspired polymerization of a His-rich peptide, yielded artificial mussel glue proteins, where β-sheets can be triggered to mimic both adhesive motifs and cohesion control mechanisms of the mussel adhesive apparatus.