Research Area

Despite the wealth of information about the adhesive proteins and the collagenous fibers in the thread of the mussel holdfast, little is understood about the junction between the two.  A current hypothesis proposes that a protein known as mussel foot protein 4 (mfp-4) serves as a bridge between collagens in the thread and proteins in the adhesive plaque. Mfp-4 contains two domains that each consist of tandemly repeated sequences with elevated levels of either histidine or aspartic acid/asparagine to selectively chelate divalent cations in order to form non-covalent crosslinks at the interface between the plaque and the thread. My research plans are to investigate metal-mediated interactions at the interface using a combination of atomic force microscopy, quartz crystal microbalance and Raman spectroscopy. Information gained from this research may provide a platform for the development of mechanically robust, biocompatible materials.