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The fouling marine mussel Mytilus edulis attaches itself to various substrates by spinning byssal threads, the adhesive discs of which are rich in the amino acid 3,4-dihydroxyphenylalanine (dopa). An acid-soluble protein was extracted and purified from the phenol gland located in the byssus-secreting foot of the animal. This protein is highly basic and contains large amounts of lysine, dopa, and 3- and 4-hydroxyproline. The composition of this protein and its sticky tendencies in vitro strongly suggest that it contributes to byssal adhesion.
Waite et al. (Fri,) studied this question.