From Biology to material - enzyme-controlled adhesives
In contrast to industrially manufactured materials, there are various organisms in nature that adhere strongly to surfaces even under the most adverse conditions. One of the most prominent examples of this is the marine mussel, in which the unnatural amino acid L-dihydroxyphenylalanine (L-Dopa) is the main binding motif. The polyphenolic proteins of the adhesive mussel byssus are non-toxic, have a low immunogenicity and are biodegradable, which is why there is great interest in Medicine, economy and industry. In recent decades, peptide-polymer conjugates have moved into the focus of many pharmaceutical and materials science tasks due to their structural diversity and functionality. [2] In this regard, the combination of mussel-inspired peptides with synthetic polymers represents a promising approach for the generation of effective adhesives, coatings and adhesive hydrogels. [3, 4] The peptide domain enables the formation of specific interactions with the target surface, while the polymer determines the adhesive function of the bioconjugate. To date, however, the de novo design of mussel-inspired peptide sequences, which enable an effective coating or gluing even under seawater conditions, has been a major challenge. With the help of the biocombinational method phage display, however, peptide sequences could be obtained, which the adhesive function of the clam foot can imitate. [5] The methodology opens up the possibility of generating non-natural peptide adhesion domains, which not only imitate nature, but also have improved properties compared to peptide domains from the binding proteins of marine mussels.
[1] Stewart, RJ, Ransom, TC & Hlady, V.,
J. Polym. Sci. A2 49 (11), 757-771 (2011).
[2] Lutz, J.-F. & Börner, HG,
Prog. Polym. Sci. 33 (1), 1-39 (2008).
[3] Wilke, P. & Borner, HG,
ACS Macro Lett., 1 (7), 871-875 (2012).
[4] Wilke, P. & Börner, HG,
Eur. Pol. J., 62, 374-379 (2015).
[5] Wilke, P., Helfricht, N., Mark., A., Papastavrou, G., Faivre, D. & Borner, HG,
J. Am. Chem. Soc., 136 (36), 12667-12674 (2014).
