Sea star-inspired recombinant adhesive proteins self-assemble and adsorb on surfaces in aqueous environments to form cytocompatible coatings.

Sea stars adhere to various underwater substrata using an efficient protein-based adhesive secretion. The protein Sfp1 is a major component of this secretion. In the natural glue, it is cleaved into four subunits (Sfp1 Alpha, Beta, Delta and Gamma) displaying specific domains which mediate protein-protein or protein-carbohydrate interactions. In this study, we used the bacterium E. coli to produce recombinantly two fragments of Sfp1 comprising most of its functional domains: the C-terminal part of the Beta subunit (rSfp1 Beta C-term) and the Delta subunit (rSfp1 Delta). Using native polyacrylamide gel electrophoresis and size exclusion chromatography, we show that the proteins self-assemble and form oligomers and aggregates in the presence of NaCl. Moreover, they adsorb onto glass and polystyrene upon addition of Na

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Declaration of Competing Interest The authors declare that they have no known competing financial interests or personal relationships that could have appeared to influence the work reported in this paper.