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. 2019 Jan 10;10:116. doi: 10.1038/s41467-018-08030-y

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© The Author(s) 2019

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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Fig. 2 — Binding characterization and stability measurements of individual histone RNA aptamer sequences. a Binding kinetic rate constants (k_a and K_D) determined for aptamers KU7 (left panels) and KU9 (right panels) binding to CTH (top panels), H4 (middle panels) and BSA (bottom panels). Aptamers concentrations tested: 100 nM (blue), 50 nM (black), 25 nM (red), 12.5 nM (green), 10 nM (magenta). b Serum stability measurements for aptamers KU7 and KU9 (5 μM) in 50% human serum. T_1/2 KU7 = 150 h. T_1/2 KU9 = 48 h