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. 2020 Oct 30;10:18718. doi: 10.1038/s41598-020-75561-0

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© The Author(s) 2020

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 licence, and indicate if changes were made. The images or other third party material in this article are included in the article's Creative Commons licence, unless indicated otherwise in a credit line to the material. If material is not included in the article's Creative Commons licence 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 licence, visit http://creativecommons.org/licenses/by/4.0/.

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Dissociation constants for the binding of K8- and K16-peptides to PS. The binding experiment was performed as described in Fig. 2 and “Methods”. The resulting data were fitted to a Langmuir isotherm to determine the dissociation constants (Kds) and the maximum binding capacities (Bmaxs) for the binding of K8- and K16-peptides to phosphatidylserine (PS).