| 초록 |
Metal complexation plays many important roles in biological systems and biomaterials. 3,4-Dihydroxyphenylalanine (Dopa), a key molecule involved in underwater mussel adhesion, strongly binds to Fe3+ ions and forms Dopa-Fe3+ complexations, which provide mechanical properties through strong cohesion. Here, we investigated the Dopa-Fe3+ complexation of mussel adhesive protein (MAP) type 3 fast variant and type 5, both of which are located at the plaque-substrate interface. Through surface forces apparatus analysis, we observed strong surface adhesion due to a high Dopa content at low pH, which is similar to the local acidified environment present during the secretion of MAPs. In higher pH conditions similar to seawater, strong cohesion by Dopa-Fe3+ complexation and dramatic decreases in surface adhesion were simultaneously observed. Our findings suggest a possible mussel adhesion mechanism at the plaque-substrate interface and might provide an exquisite and sophisticated strategy for designing mussel mimicking biomaterials with targeted applications. |
