posted on 2018-08-02, 00:00authored byJia Wang, Thomas Scheibel
The
underwater adhesion of marine mussels is a fascinating example
of how proteinaceous adhesives, although water-soluble to begin with,
can be used in seawater. Marine mussels adhere to the substrate via
adhesive plaques, where the adhesive proteins are located especially
at the substratum’s interface. One major compound of the adhesives
in Mytilidae is the mussel foot protein 3b (mfp-3b). Here, recombinant
mfp-3b (rmfp-3b) was produced in Escherichia coli. rmfp-3b showed upper critical solution temperature (UCST) mediated
complex coacervation at pH 3.0 in the presence of citrate yielding
a liquid–liquid phase separation. Further, the rmfp-3b coacervation
could also be induced in seawater conditions such as the respective
pH and ionic strength, but without UCST behavior. In particular, sulfate
and citrate anions could significantly induce complex coacervation.
This study provides insights into the molecular behavior of one of
the key proteins of mussels involved in underwater adhesion and may
inspire new applications of bioadhesives using recombinant mussel
foot proteins.