3 years ago

Tuning underwater adhesion with cation–π interactions

Tuning underwater adhesion with cation–π interactions
J. Herbert Waite, Wei Wei, Thomas R. Cristiani, Bradley F. Chmelka, Alex M. Schrader, Howard A. Dobbs, Jacob N. Israelachvili, Matthew Idso, Matthew A. Gebbie
Cation–π interactions drive the self-assembly and cohesion of many biological molecules, including the adhesion proteins of several marine organisms. Although the origin of cation–π bonds in isolated pairs has been extensively studied, the energetics of cation–π-driven self-assembly in molecular films remains uncharted. Here we use nanoscale force measurements in combination with solid-state NMR spectroscopy to show that the cohesive properties of simple aromatic- and lysine-rich peptides rival those of the strong reversible intermolecular cohesion exhibited by adhesion proteins of marine mussel. In particular, we show that peptides incorporating the amino acid phenylalanine, a functional group that is conspicuously sparing in the sequences of mussel proteins, exhibit reversible adhesion interactions significantly exceeding that of analogous mussel-mimetic peptides. More broadly, we demonstrate that interfacial confinement fundamentally alters the energetics of cation–π-mediated assembly: an insight that should prove relevant for diverse areas, which range from rationalizing biological assembly to engineering peptide-based biomaterials.

Publisher URL: http://dx.doi.org/10.1038/nchem.2720

DOI: 10.1038/nchem.2720

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