Abstract
Mussel foot proteins (Mfps) exhibit remarkably adaptive adhesion and bridging between polar surfaces in aqueous solution despite the strong hydration barriers at the solid-liquid interface. Recently, catechols and amines-two functionalities that account for >50 mol % of the amino acid side chains in surface-priming Mfps-were shown to cooperatively displace the interfacial hydration and mediate robust adhesion between mineral surfaces. Here we demonstrate that (1) synergy between catecholic and guanidinium side chains similarly promotes adhesion, (2) increasing the ratio of cationic amines to catechols in a molecule reduces adhesion, and (3) the catechol-cation synergy is greatest when both functionalities are present within the same molecule.
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