Nagafuchi T
Department of Orthopaedic Surgery, Jikei University School of Medicine, Tokyo, Japan.
Nihon Seikeigeka Gakkai Zasshi. 1992 Nov;66(11):1176-83.
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.
海洋贻贝紫贻贝（Mytilus edulis L.）中被称为“多酚蛋白（ppp）”的蛋白质经过特殊进化，使贻贝能够牢固地附着在海洋中的固体表面，在将这种软体动物固定在海洋岩石上发挥着重要作用。在本研究中，对ppp在“潮湿环境”中的粘附机制进行了研究。ppp对玻璃和聚丙烯的吸附非常迅速，在10分钟内达到饱和。当ppp浓度较低时，它在玻璃表面形成单层，其对表面的亲和力与通常被认为对固体表面具有强亲和力并用作细胞粘合剂的聚-D-赖氨酸一样大。另一方面，当ppp浓度超过5.0×10（-3）μmol/ml时，观察到对玻璃的多层吸附。此外，当ppp用酪氨酸酶修饰时，发生分子间缩合，这通过ppp分子的多巴和赖氨酸残基之间的交联有助于形成刚性粘附。这些发现为开发用于活体组织的新型粘合剂提供了重要信息。
