| 초록 |
Mussels are interesting marine creatures maintaining their lives on various substrates such as metal or mineral surfaces in the ocean. Intensive researches about mussel adhesion found out that L-3,4-dihydroxyphenylalanine (DOPA) is a key molecule in underwater adhesion. Many studies have shown that DOPA is directly related to adhesion. However, DOPA is vulnerable to oxidation with high pH and quinone, its oxidative form in high pH, contributes to cohesion rather than adhesion. Appropriate balance between surface adhesion and cohesion is crucial issue in most adhesives. However, there are no studies on reasonable mechanism about such balance regulations in mussels. Foot protein type 6 (fp-6) in Mytilus californianus has been reported as an antioxidant of DOPA due to high mol percent of cysteine residues. In this presentation, we suggest a novel hypothesis about redox regulation of DOPA and the role of fp-6 in DOPA chemistry using in vivo residue specific incorporated recombinant proteins. This study will give a new clue about understanding of mussel adhesion and can be applied to the development of various adhesive biomaterials including mussel-inspired chemical glues. |
