Over het archief
Het OWA, het open archief van het Waterbouwkundig Laboratorium heeft tot doel alle vrij toegankelijke onderzoeksresultaten van dit instituut in digitale vorm aan te bieden. Op die manier wil het de zichtbaarheid, verspreiding en gebruik van deze onderzoeksresultaten, alsook de wetenschappelijke communicatie maximaal bevorderen.
Dit archief wordt uitgebouwd en beheerd volgens de principes van de Open Access Movement, en het daaruit ontstane Open Archives Initiative.
Basisinformatie over ‘Open Access to scholarly information'.
Disentangling the roles of functional domains in the aggregation and adsorption of the multimodular sea star adhesive protein Sfp1
Lefevre, M.; Ederth, T.; Masai, T.; Wattiez, R.; Leclère, P.; Flammang, P.; Hennebert, E. (2021). Disentangling the roles of functional domains in the aggregation and adsorption of the multimodular sea star adhesive protein Sfp1. Mar. Biotechnol. 23(5): 724-735. https://dx.doi.org/10.1007/s10126-021-10059-y
In: Marine Biotechnology. Springer-Verlag: New York. ISSN 1436-2228; e-ISSN 1436-2236, meer
|  |
| Trefwoorden |
Asteroidea [WoRMS]
Marien/Kust |
| Author keywords |
Sea stars; Adhesive protein; Sfp1; Functional domain; Adsorption; SPR |
| 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 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. |
IMIS is ontwikkeld en wordt gehost door het VLIZ.
