Application Note #157
Sea anemone actinoporins (pore forming toxins) bind to the lipid membrane causing cell death. Equinatoxin II (EqtII), fragaceatoxin C (FraC), sticholysin II (StnII) and sticholysin I (StnI) binding to lipid vesicles were measured using MP-SPR.
Pore forming toxins are a protein family which interacts with the cell membrane causing hemolytic pores that are lethal for their target cells. In water the proteins are firmly folded but upon interaction with the cell membrane lipids, they become oligomeric integral membrane structures. The binding of toxins depends on the membrane structure.
Multi-Parametric Surface Plasmon Resonance (MP-SPR) is a highly sensitive and label-free method used to study surface changes. Lipid vesicle layers were spread on a sensor surface and four sea anemone actinoporins interactions on lipids were measured. Sticholysin I and II had clearly higher binding and pore forming ability when compared to other two actinoporins. Cholesterol in the lipid structure was found to increase the binding of equinatoxin II and fragaceatoxin C.
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- If you are interested in reading more, see AN#139 about conformation of lipid layers, AN#152 about interactions of lipid vesicles and AN#151 about measurement of soft and hard corona on nanoparticle in 100% serum.
- Have a look at publications about pore forming toxins: Garcia-Linares et al. (2016), Palacios-Ortega et al. (2016) and Garcia-Linares et al. (2016)
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