Mussel adhesives residues

Conversion of the Microbially Produced Preadhesive to an Adhesive Protein. The polyphenolic protein purified from yeast adheres to a wide variety of surfaces including glass and plastic. The adherence probably results from the presence of many polar residues capable of hydrogen bonding and lysine residues that can form ionic interactions. However, this protein does not generate water-resistant bonds to surfaces nor does it have cohesive strength. For those purposes, it is necessary to convert at least a portion of the tyrosine residues to dopa and permit crosslink formation to occur after surface adhesion is achieved. That is, it is necessary to mimic the natural mussel process in which the dopa form of the polyphenolic protein is applied and then rapidly... 

Tyrosinase was reported to hydroxylate and oxidize tyrosine residues in proteins1231, which is important in the production of moisture-resistant adhesives. In fact, tyrosinase has been used for the production of synthetic glues with similar compositions to those of naturally occurring adhesives such as mussel glue1241. 

A more recent example of a biotransformation of peptide-polymer conjugates combines biocombinatorial procedures with enzjonatic activation processes in order to realize mussel-glue inspired adhesion. Phage-display biopanning incorporating tyrosinase to transform L-tyrosine residues to L-dopa enabled the direct selection of enzymatically activable 12-mer peptide adhesion domains for aluminum oxide (Figure 1.21). 

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