Pohang University of Science and Technology (POSTECH) researchers have verified the secret to the strong surface adhesion of mussel adhesive proteins (MAPs) even in an environment that causes oxidation.
The research team was led by Professor Hyung Joon Cha, Dr. Mincheol Shin, and Ph.D. candidate Taehee Yoon (Department of Chemical Engineering).
Dopa Limiting MAP’s Application
MAP is gaining attention as a biomedical material used as a bioadhesive or a drug delivery system as it is nature-derived and harmless to the body. However, there was a limitation in that Dopa, a major component of the mussel adhesive protein, is easily oxidized which leads to weakening of the surface adhesion.
The research team focused on the fact that among the surface proteins of mussels, cysteine-rich proteins are involved in oxidation and reduction. When Dopa was oxidized to Dopa quinone with weakened adhesion, the research team added protein type 6 (fp-6) that contains cysteine, which changes the Dopa quinone into △Dopa. △Dopa is a tautomer1 of Dopa quinone and has a very strong surface adhesion like Dopa.
Adding Cysteine-rich Protein Increases Adhesion
The research team also verified that when △Dopa is formed in the protein, it can have a stronger surface adhesion than Dopa.
This study is the first study to verify that the fp-6 shifts the tautomer equilibrium of oxidized Dopa to make mussels stick strongly to surfaces even in oxidative underwater conditions. Applying these findings to the Dopa-based underwater adhesive can increase its surface adhesion.
Professor Hyung Joon Cha explained, “We have verified for the first time that the cysteine-rich surface protein, conventionally known to block the oxidation of Dopa, also promotes the change into △Dopa, which helps to maintain the adhesion in mussels even in oxidative underwater environments.”
This study was conducted with the support of the Basic Research Program of the National Research Foundation of Korea.
1. Tautomer
A compound that has the same molecular formula but does not have the same structure or spatial arrangement of components in the molecule.
加载中...
