[Mechanism of adhesion of polyphenolic protein and its potential for clinical application].

The protein of the marine mussel Mytilus edulis L. known as "polyphenolic protein (ppp)" evolved specifically to allow mussels to attach strongly to solid surfaces in the sea and plays an important role in anchoring this mollusc to ocean rocks. In the present study, the mechanism of the adhesiveness of ppp in a "wet environment" was investigated. The adsorption of ppp to both glass and polypropylene was very rapid, and it reached saturation within 10 minutes. When the concentration of ppp was low, it formed a monolayer on glass surfaces, and its affinity for the surface proved to be as great as that of poly-D-lysine which is generally considered to have a strong affinity for solid surfaces and is applied as a cell adhesive. On the other hand, when the ppp concentration exceeded 5.0 x 10(-3) mumol/ml, multilayer adsorption to glass was observed. Moreover, when ppp was modified by tyrosinase, intermolecular condensation occurred which was contributed to a rigid adhesion by cross-linking between the dopa and lysine residues of ppp molecules. These findings provide important information on the development of a new type of adhesive for use on living tissues.