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.