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Nat Chem. 2017 May;9(5):473-479. doi: 10.1038/nchem.2720. Epub 2017 Feb 13.

Tuning underwater adhesion with cation-π interactions.

Author information

1
Materials Department, University of California, Santa Barbara, California 93106, USA.
2
Materials Research Laboratory, University of California, Santa Barbara, California 93106, USA.
3
Department of Molecular, Cell and Developmental Biology, University of California, Santa Barbara, California 93106, USA.
4
Department of Chemical Engineering, University of California, Santa Barbara, California 93106, USA.

Abstract

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.

PMID:
28430190
DOI:
10.1038/nchem.2720
[Indexed for MEDLINE]
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