Implementing Zn<sup>2+</sup> ion and pH-value control into artificial mussel glue proteins by abstracting a His-rich domain from preCollagen.
basic_science · Level V
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- Record sourced from PubMed, PMID 33596288.
- Also identified by DOI 10.1039/d0sm02118k.
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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 β-sheet formation. The artificial constructs show strong adsorption to Al2O3, the resulting coatings tolerate hypersaline conditions and cohesion is improved by activating the β-sheet formation, that enhances E-modulus up to 60%.
Medical subject headings
- Dihydroxyphenylalanine
- Protein Conformation, beta-Strand