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. 2017 Nov 27;7:16329. doi: 10.1038/s41598-017-16426-x

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© The Author(s) 2017

Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/.

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Binding stability of Ts1-S14R-Bodipy characterized by LRET using DI-3GLBT-R(-5). (a) Time constant of DA signals (red squares) are accelerated as the concentration of Ts1-S14R-Bodipy is increased, whereas that of SE signals (green circles) show a fixed value, around 1.4 ms (0 µM and 0.25 µM: n = 8; 0.5 µM: n = 6; 1 µM: n = 6; and, 2 µM: n = 4). The apparent dose-response curve of DA signals indicate that the proportion of Ts1-S14R-Bodipy binding to DI-3GLBT-R(-5) reach 50% at around 0.5 µM and reach 100% at around 1 µM. (b) The dissociation rate of Ts1-S14R-Bodipy as a function of time in toxin-free solution is very slow. We evaluated the binding fraction of Ts1-S14R-Bodipy by the amplitude of SE signals (n = 8). At 40 minutes after pretreatment by Ts1-S14R-Bodipy, 85% of the molecules are still bound. (c) Representative raw traces of SE signal at Time 0 min (green) and at Time 40 min (orange) in B.