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. 2017 Jun 7;7:2968. doi: 10.1038/s41598-017-02916-5

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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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ML290 and binding of ¹²⁵I-H2 relaxin to RXFP1 stably expressed in HEK293 cells. In (A) co-incubation with ML290 (90 min), increased total binding of ¹²⁵I-H2 relaxin to RXFP1 in a concentration-dependent manner (n = 6). In (B) ML290 (1 μM) had no significant effect on competition by H2 relaxin for ¹²⁵I-H2 relaxin binding (n = 8). In kinetic studies, ML290 (1 μM) had no significant effect on (C) dissociation (n = 3) or (D) association rate (n = 6–7) of ¹²⁵I-H2 relaxin from RXFP1. Data are mean ± SEM of ‘n’ experiments.