Sea stars can adhere to various underwater substrata using an adhesive secretion of which Sfp1 is a major component. Sfp1 is a multimodular protein composed of four subunits (Sfp1 Alpha, Beta, Delta, and Gamma) displaying different functional domains. We recombinantly produced 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). Surface plasmon resonance analyses of protein adsorption onto different model surfaces showed that rSfp1 Beta C-term exhibits a significantly higher adsorption than the fibrinogen control on hydrophobic, hydrophilic protein-resistant, and charged self-assembled monolayers, while rSfp1 Delta adsorbed more on negatively charged and on protein-resistant surfaces compared to fibrinogen. Truncated recombinant rSfp1 Beta C-term proteins were produced in order to investigate the role of the different functional domains in the adsorption of this protein. The analysis of their adsorption capacities on glass showed that two mechanisms are involved in rSfp1 Beta C-term adsorption: (1) one mediated by the EGF-like domain and involving Ca²⁺ and Mg²⁺ ions, and (2) one mediated by the sequence of Sfp1 Beta with no homology with known functional domain in databases, in the presence of Na⁺, Ca²⁺ and Mg²⁺ ions.

海星可以使用粘性分泌物粘附在各种水下基质上，其中 Sfp1 是主要成分。Sfp1 是一种多模块蛋白，由显示不同功能域的四个亚基（Sfp1 Alpha、Beta、Delta 和 Gamma）组成。我们重组产生了 Sfp1 的两个片段，包括其大部分功能域：Beta 亚基的 C 端部分 (rSfp1 Beta C-term) 和 Delta 亚基 (rSfp1 Delta)。蛋白质吸附到不同模型表面的表面等离子共振分析表明，rSfp1 Beta C-term 在疏水性、亲水性蛋白质抗性和带电自组装单层上表现出比纤维蛋白原对照显着更高的吸附，而 rSfp1 Delta 在带负电荷的单层上吸附更多与纤维蛋白原相比，在抗蛋白质的表面上。产生截短的重组 rSfp1 Beta C 端蛋白，以研究不同功能域在该蛋白吸附中的作用。对它们在玻璃上的吸附能力的分析表明，rSfp1 Beta C-term 吸附涉及两种机制：（1）一种由 EGF 样结构域介导并涉及 Ca²⁺和 Mg ²⁺离子，以及 (2) 在 Na ⁺、Ca ²⁺和 Mg ²⁺离子存在下，由 Sfp1 Beta 序列介导的一种，与数据库中的已知功能域没有同源性。