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. 2019 Aug 7;11(8):462. doi: 10.3390/toxins11080462

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© 2019 by the authors.

Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (http://creativecommons.org/licenses/by/4.0/).

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Binding of lysenin to sphingomyelin-containing liposomes. (A) Lipid-overlay assay revealed selective recognition of SM by recombinant lysenin^WT and lysenin^V88C/Y131C. (B) Surface Plasmon Resonance (SPR) sensorgrams of the binding of lysenin^WT (), lysenin^V88C/Y131C (●●●), and lysenin^V88C/Y131C with 10 mM 1,4-Dithiothreitol (DTT) (▬ ▬) to SM-containing liposomes (composed of SM/1,2-dioleoyl-sn-glycero-3-phosphocholine (DOPC)/cholesterol) that were immobilized on the surface of an L1 sensor chip. Sensorgrams were performed in triplicate, and one representative experiment is shown.

Inline graphic — Binding of lysenin to sphingomyelin-containing liposomes. (A) Lipid-overlay assay revealed selective recognition of SM by recombinant lysenin^WT and lysenin^V88C/Y131C. (B) Surface Plasmon Resonance (SPR) sensorgrams of the binding of lysenin^WT (), lysenin^V88C/Y131C (●●●), and lysenin^V88C/Y131C with 10 mM 1,4-Dithiothreitol (DTT) (▬ ▬) to SM-containing liposomes (composed of SM/1,2-dioleoyl-sn-glycero-3-phosphocholine (DOPC)/cholesterol) that were immobilized on the surface of an L1 sensor chip. Sensorgrams were performed in triplicate, and one representative experiment is shown.