Direct Observation of the Interplay of Catechol Binding and Polymer Hydrophobicity in a Mussel-Inspired Elastomeric Adhesive.

ABSTRACT: Marine organisms such as mussels have mastered the challenges in underwater adhesion by incorporating post-translationally modified amino acids like l-3,4-dihydroxyphenylalanine (DOPA) in adhesive proteins. Here we designed a catechol containing elastomer adhesive to identify the role of catechol in interfacial adhesion in both dry and wet conditions. To decouple the adhesive contribution of catechol to the overall adhesion, the elastomer was designed to be cross-linked through [2 + 2] photo-cycloaddition of coumarin. The elastomer with catechol moieties displayed a higher adhesion strength than the catechol-protected elastomer. The contact interface was probed using interface-sensitive sum frequency generation spectroscopy to explore the question of whether catechol can displace water and bond with hydrophilic surfaces. The spectroscopy measurements reveal that the maximum binding energy of the catechol and protected-catechol elastomers to sapphire substrate is 7.0 ± 0.1 kJ/(mole of surface O-H), which is equivalent to 0.10 J/m². The higher dry and wet adhesion observed in the macroscopic adhesion measurements for the catechol containing elastomer originates from multiple hydrogen bonds of the catechol dihydroxy groups to the surface. In addition, our results show that catechol by itself does not remove the confined interstitial water. In these elastomers, it is the hydrophobic groups that help in partially removing interstitial water. The observation of the synergy between catechol binding and hydrophobicity in enabling the mussel-inspired soft adhesive elastomer to stick underwater provides a framework for designing materials for applications in tissue adhesion and moist-skin wearable electronics.

SUBMITTER: Kaur S 

PROVIDER: S-EPMC6202650 | biostudies-literature | 2018 Oct

REPOSITORIES: biostudies-literature