at Google ScholarTitle data
Lefevre, Mathilde ; Flammang, Patrick ; Aranko, A.Sesilja ; Linder, Markus B. ; Scheibel, Thomas ; Humenik, Martin ; Leclercq, Maxime ; Surin, Mathieu ; Tafforeau, Lionel ; Wattiez, Ruddy ; Leclèrc, Philippe ; Hennebert, Elise:
Sea star-inspired recombinant adhesive proteins self-assemble and adsorb on surfaces in aqueous environments to form cytocompatible coatings.
In: Acta Biomaterialia.
Vol. 112
(2020)
.
- pp. 62-74.
ISSN 1878-7568
DOI: https://doi.org/10.1016/j.actbio.2020.05.036
Abstract in another language
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+ and/or Ca2+ ions, forming homogeneous coatings or irregular meshworks, depending on the cation species and concentration. We show that coatings made of each of the two proteins have no cytotoxic effects on HeLa cells and even increase their proliferation. We propose that the Sfp1 recombinant protein coatings are valuable new materials with potential for cell culture or biomedical applications.