ABSTRACT
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 Zn2+ induced ß-sheet formation. The artificial constructs show strong adsorption to Al2O3, the resulting coatings tolerate hypersaline conditions and cohesion is improved by activating the ß-sheet formation, that enhances E-modulus up to 60%.
Subject(s)
Dihydroxyphenylalanine , Protein Conformation, beta-Strand , Animals , Bivalvia , Hydrogen-Ion Concentration , ZincABSTRACT
The formation of cysteinyldopa as biogenic connectivity in proteins is used to inspire a chemical pathway toward mussel-adhesive mimics. The mussel-inspired polymerization (MIPoly) exploits the chemically diverse family of bisphenol monomers that is oxidizable with 2-iodoxybenzoic acid to give bisquinones. Those react at room temperature with dithiols in Michael-type polyadditions, which leads to polymers with thiol-catechol connectivities (TCC). A set of TCC polymers proved adhesive behavior even on challenging poly(propylene) substrates, where they compete with commercial epoxy resins in dry adhesive strength. MIPoly promises facile scale up and exhibits high modularity to tailor adhesives, as proven on a small library where one candidate showed wet adhesion on aluminum substrates in both water and sea water models.