Mussel adhesive proteins (MAPs) have received increased attention as potential environmentally friendly adhesives under aqueous conditions and in medicine. However, attempts to produce functional recombinant MAPs (mainly foot protein type 1, fp-1) by several expression systems have failed. Even though we previously reported a functional expression of recombinant foot protein type 5 (fp-5) with significant adhesive ability in Escherichia coli, its practical use was limited by several problems. Here, to overcome these limitations, we designed and constructed the novel hybrid mussel bioadhesive fp-151, a fusion protein comprising six fp-1 decapeptide repeats at each fp-5 terminus. Using micro- and bulk-scale characterization and cell-adhesion analyses, we demonstrate that fp-151 has the potential to be a revolutionary and practical bioadhesive with strong adhesive ability, a simple purification process, proper manipulation properties, and high biocompatibility.

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