[Abstract]

Although Dopa-Fe3+ complexation is known to play an important role in mussel adhesion for providing mechanical properties, its function at the plaque/substrate interface, where actual surface adhesion occurs, remains unknown, with regard to interfacial mussel adhesive proteins (MAPs) type 3 fast variant (fp-3F) and type 5 (fp-5).
Here, we confirmed Dopa-Fe3+ complexation of interfacial MAPs and investigated the effects of Dopa-Fe3+ complexation regarding both surface adhesion and cohesion. The force measurements using surface forces apparatus (SFA) analysis showed that intrinsic strong surface adhesion at low pH, which is similar to the local acidified environment present during the secretion of adhesive proteins, vanishes by Dopa-Fe3+ complexation and alternatively, strong cohesion is generated in higher pH conditions similar to seawater. A high Dopa content increased the capacity for both surface adhesion and cohesion, but not at the same time. In contrast, a lack of Dopa resulted in both weak surface adhesion and cohesion without significant effects of Fe3+ complexation.
Our findings shed light on how mussels regulate Dopa functionality at the plaque/substrate interface, in response to the microenvironment, and might provide new insight for the design of mussel-inspired biomaterials.

DOI: 10.1021/acs.chemmater.6b03676

LINK: http://pubs.acs.org/doi/abs/10.1021/acs.chemmater.6b03676