Revisiting the adhesion mechanism of mussel-inspired chemistry.

ABSTRACT: Mussel-inspired chemistry has become an ideal platform to engineer a myriad of functional materials, but fully understanding the underlying adhesion mechanism is still missing. Particularly, one of the most pivotal questions is whether catechol still plays a dominant role in molecular-scale adhesion like that in mussel adhesive proteins. Herein, for the first time, we reveal an unexplored adhesion mechanism of mussel-inspired chemistry that is strongly dictated by 5,6-dihydroxyindole (DHI) moieties, amending the conventional viewpoint of catechol-dominated adhesion. We demonstrate that polydopamine (PDA) delivers an unprecedented adhesion of 71.62 mN m^-1, which surpasses that of many mussel-inspired derivatives and is even 121-fold higher than that of polycatechol. Such a robust adhesion mainly stems from a high yield of DHI moieties through a delicate synergy of leading oxidation and subsidiary cyclization within self-polymerization, allowing for governing mussel-inspired adhesion by the substituent chemistry and self-polymerization manner. The adhesion mechanisms revealed in this work offer a useful paradigm for the exploitation of functional mussel-inspired materials.

SUBMITTER: Zhang C 

PROVIDER: S-EPMC8827048 | biostudies-literature | 2022 Feb

REPOSITORIES: biostudies-literature