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. 2019 Sep 17;9:13446. doi: 10.1038/s41598-019-49758-x

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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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The effect of peptide P3 is BMP and cell type-dependent. (A) Representative pSmad1/5 immunoblot of protein extracts from HMEC-1 treated with peptide P3, P3r, P3rpro P4 and P5 (at 250 μM) with or without BMP9 (at 0.03 ng/ml, or 1.24 pM GFD dimer) or BMP4 (at 0.3 ng/ml, or 11.54 pM GFD dimer). Quantification of pSmad1/5 from three independent experiment is shown below. N = 3. Data shown as means ± S.E. In the BMP4-treated group, paired t-tests against BMP4-treated control were performed, and those with P values < 0.05 are shown. (B) Effect of peptide P3 and control peptides (at 160 μM) on BMP4 (3 ng/ml, or 115.4 pM GFD dimer) stimulated gene induction of ID1 and HEY1 in HMEC-1, N = 4. Data shown as means ± S.E., paired t-tests against BMP4-treated control, and those with P values < 0.05 are shown. (C,D) SPR sensorgrams of BMP4 binding to ALK3-Fc in the presence of peptide P3 (C) or P3r (D) at various concentrations on an ALK3-Fc coated CM5 chip. Plots of the maximum binding levels (indicated by the arrows) against peptide concentrations are shown below each graph respectively. (E) Effect of peptide P3 and control peptides (at 160 μM) on BMP9-induced ALP activity in C2C12 cells. Data were obtained from three independent experiments, with duplicated wells for each treatment condition in a single experiment. Data shown as means ± S.E.