ArticleMarine biotechnology (New York, N.Y.)2021
Disentangling the Roles of Functional Domains in the Aggregation and Adsorption of the Multimodular Sea Star Adhesive Protein Sfp1.
Article in Marine biotechnology (New York, N.Y.), 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
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Who cites it
5 citing papers in PubMed, 6 citations in OpenAlex.
- Recombinant Proteins: A Molecular Tool to Understand Marine Adhesion and to Advance Biomaterials.Advanced healthcare materials · 2026Review
- Amyloid-like Structures in Marine Adhesive Proteins.Marine drugs · 2025Review
- The Involvement of Cell-Type-Specific Glycans inBiomimetics (Basel, Switzerland) · 2022Article
- In the footsteps of sea stars: deciphering the catalogue of proteins involved in underwater temporary adhesion.Open biology · 2022Article
- (Un)expected Similarity of the Temporary Adhesive Systems of Marine, Brackish, and Freshwater Flatworms.International journal of molecular sciences · 2021Article
Corrections and comments
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Authors and funding
7 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
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 Ca
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Registered trials
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